1887

Color Plates

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.
  • HTML
    18.85 Kb
  • XML
    16.98 Kb
Add to My Favorites
You must be logged in to use this functionality
Loading full text...

Full text loading...

/deliver/fulltext/10.1128/9781555816544/notes.html?itemId=/content/book/10.1128/9781555816544.notes&mimeType=html&fmt=ahah

Figures

Image of COLOR PLATE 1

Click to view

COLOR PLATE 1

(Chapter 1) (Top) Model of ferric enterobactin based on the crystal structure of vanadium( IV) enterobactin (left), and structure of ferric corynebactin as deduced from circular dichroism spectra and computer modeling (right). (Middle) Viewed down the pseudo-three-fold axis, the chirality of each metal center can be seen. Ferric enterobactin is Δ, while ferric corynebactin is Λ. Also apparent from this view is the difference in geometry around the iron center. While ferric corynebactin is nearly octahedral, ferric enterobactin is distorted toward a trigonal prismatic geometry. Note that only the ferric tris(catechol) center is colored. The three oxygen atoms on the front face of the octahedron are red; the three oxygen atoms on the back face are dark red. (Bottom) Under each structure is a schematic drawing that shows the molecular conformation.

Citation: Crosa J, Mey A, Payne S. 2004. Color Plates, In Iron Transport in Bacteria. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of COLOR PLATE 2

Click to view

COLOR PLATE 2

(Chapter 1) Structural comparisons show the preorganization of alcaligin for metal binding. The structure of the free ligand (at left) is essentially the same as for the FeL metal complex. The root mean square deviation in atom positions is 0.227Å. The structure of the dimeric FeL complex (at right) requires that the central ring twist from its ground state structure, which is preorganized to bind a common metal center, in order to bridge two metal ions. The cartoon illustrates this effect and is a reminder that the word “chelate” is derived from chelos, or crab's claw.

Citation: Crosa J, Mey A, Payne S. 2004. Color Plates, In Iron Transport in Bacteria. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of COLOR PLATE 3

Click to view

COLOR PLATE 3

(Chapter 1) Crystal structure of Fe(III) ferrioxamine B. The structure shown has a Δ chirality.

Citation: Crosa J, Mey A, Payne S. 2004. Color Plates, In Iron Transport in Bacteria. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of COLOR PLATE 4

Click to view

COLOR PLATE 4

(Chapter 1) (Left) Crystal structure of Fe(III) ferrichrome A. Due to disorder of two of the three methylglutaconic acid moieties and one seryl hydroxyl group, the original crystal structure was incomplete. These moieties were added into this Figure for clarity. (Right) A view down the pseudo-threefold axis showing the Δ chirality of the complex. Note that only the ferric tris(catechol) center is colored. The three oxygen atoms on the front face of the octahedron are red; the three oxygen atoms on the back face are dark red.

Citation: Crosa J, Mey A, Payne S. 2004. Color Plates, In Iron Transport in Bacteria. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of COLOR PLATE 5

Click to view

COLOR PLATE 5

(Chapter 4) Crystal structures of FecA (left), FhuA (middle), and FepA (right). The globular domain is drawn in a different color in each structure. Reprinted from Ferguson et al. (2002) with permission from the publisher.

Citation: Crosa J, Mey A, Payne S. 2004. Color Plates, In Iron Transport in Bacteria. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of COLOR PLATE 6

Click to view

COLOR PLATE 6

(Chapter 4) Stereo view of the globular domain in FecA. The secondary structure is shown, with the helix in red, the β-strand in yellow, and the coil in green. Apices A (residue 138), B (residue 155), and C (residue 176) are indicated, as well as Arg150 and Arg196 involved in the lock region, the beginning and end of the β5-β6 loop (residues 196 and 210), the last residue of the domain (residue 223) and the first residue which could be located in the structure (residue 81). The diferric-dicitrate in the liganded structure is shown to visualize the possible channel for transport.

Citation: Crosa J, Mey A, Payne S. 2004. Color Plates, In Iron Transport in Bacteria. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of COLOR PLATE 7

Click to view

COLOR PLATE 7

(Chapter 4) Stereo view of the apices and switch helices in the three structures. The apices are indicated by residue number. The relative locations with respect to the barrel are shown, after a least-squares fit of the three structures, for FepA (blue [63, 78, 101]), FhuA (green [81, 100, 116]), and FecA (red [138, 155, 176]).

Citation: Crosa J, Mey A, Payne S. 2004. Color Plates, In Iron Transport in Bacteria. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of COLOR PLATE 8

Click to view

COLOR PLATE 8

(Chapter 4) Reference points in the structure of FecA. The view is from the bottom of the barrel. Arg150 and Arg196 of the globular domain and Glu541 and Glu587 on the barrel (red) constitute the lock region. The first residue of the barrel is also indicated. The TonB box and the possible second site of interaction with TonB are in blue, and the β5-β6 loop and strictly conserved Arg467 lining the putative channel are in green. These reference points occur in all three structures at identical locations.

Citation: Crosa J, Mey A, Payne S. 2004. Color Plates, In Iron Transport in Bacteria. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of COLOR PLATE 9

Click to view

COLOR PLATE 9

(Chapter 4) Stereo view of the possible second site of interaction with TonB in FecA. The strictly conserved residues 707 to 710, at the beginning of loop 11, are in CPK colors, and the identical Arg731, at the end of loop 11, is in blue. This structural component superposes with the corresponding structures in FepA and FhuA.

Citation: Crosa J, Mey A, Payne S. 2004. Color Plates, In Iron Transport in Bacteria. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of COLOR PLATE 10

Click to view

COLOR PLATE 10

(Chapter 6) (A) Crystal structure of HemO. The His23 ligand of the proximal helix (light and dark blue) coordinates the heme molecule (red) within the molecule. Residues Lys16 and Tyr112 coordinate the propionates of the heme molecule for regioselectivity by HemO. (B) Alignment of truncated human HO-1 (yellow) and HemO (blue), demonstrating the high degree of structural similarities. Adapted from Schuller et al. (1999 and 2001).

Citation: Crosa J, Mey A, Payne S. 2004. Color Plates, In Iron Transport in Bacteria. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of COLOR PLATE 11

Click to view

COLOR PLATE 11

(Chapter 7) Current model for TonB-dependent energy transduction. For a description, see the text. Reprinted from Postle and Kadner (2003) with permission of the publisher.

Citation: Crosa J, Mey A, Payne S. 2004. Color Plates, In Iron Transport in Bacteria. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of COLOR PLATE 12

Click to view

COLOR PLATE 12

(Chapter 8) Stereo view of the binding sites in the albomycin (a), coprogen (b), and Desferal (c) complexes. The important hydrogen bonds involved in binding each of these hydroxamate-type sideophores are labeled. Albomycin is green, coprogen is orange, and Desferal is blue in each of their respective complexes. The proportion of albomycin visible is identical to that of ferrichrome. Reprinted from Clarke, Braun, et al. (2002) with permission from the publisher.

Citation: Crosa J, Mey A, Payne S. 2004. Color Plates, In Iron Transport in Bacteria. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of COLOR PLATE 13

Click to view

COLOR PLATE 13

(Chapter 10) The FepA, FhuA, FecA, and BtuB N termini. A four-strand β-sheet is the structural basis of all four N-domains, which each contain a loop (NL1) that projects into their surface vestibules. α-Helical regions are red, β-sheets are gold, turn domains are blue, and the TonB box regions of the receptor proteins are green. Note the similarity of the FepA and FecA TonB box sequences (residues 11 to 18 and 81 to 87, respectively), which adhere to the wall of their β-barrels in the ligand-free state, and the dissimilarity of the BtuB TonB box structure (crystallographic coordinates are from the Protein Data Bank [http://www.rcsb.org/pdb]).

Citation: Crosa J, Mey A, Payne S. 2004. Color Plates, In Iron Transport in Bacteria. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of COLOR PLATE 14

Click to view

COLOR PLATE 14

(Chapter 10) Model of FeEnt transport through FepA. (Top) Formal representation of the FepA transport process. Constants 1 to 4 are experimentally defined: fluors attached to L3 reflect both the first and second binding stages ( = 0.02/s; = 0.005/s;), which are both reversible ( = 0.03/s; = 0.003/s [see the text]). (Bottom) The FepA transport cycle is depicted as a series of conformational stages that result in binding and internalization of FeEnt. The representations of FepA originated from its crystal structure, but they are postulated forms that were not crystallographically demonstrated. By analogy to FhuA and FecA, FeEnt binding may relocate the TonB-box region of FepA away from the β-barrel wall. Such movement may signal receptor occupancy to TonB, but another view is that TonB box movement away from the barrel wall allows the N-domain to dislodge from the channel. Next, the ligand passes through the C-domain channel (Transport). Theory and experiments suggest, but so far do not explicitly prove, that input of energy is required at this stage. Similarly, TonB may or may not function during this phase of the transport reaction. A variety of findings raise the possibility that the N-domain exits the pore during ligand uptake, but this idea is not fully substantiated: structural changes that facilitate ligand transport may take place in the N-domain while it is resident in the channel. After transport, the receptor re-assembles, either by reinsertion of the N-domain into the β-barrel or by structural changes in situ within the pore, another potential phase for the input of energy and/or TonB. Lastly, the loops reopen to a state of maximum receptivity to ligands.

Citation: Crosa J, Mey A, Payne S. 2004. Color Plates, In Iron Transport in Bacteria. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of COLOR PLATE 15

Click to view

COLOR PLATE 15

(Chapter 10) Crystal structures of the TonB C terminus and BtuB in the absence and presence of B12. For the TonB C terminus, helices are red and β-sheets are gold. A165, the N-terminal-most solved residue, 5 residues downstream from Q160, is red. I238, the penultimate amino acid, is green. For BtuB, the β-barrel is white, the N-domain is green, the TonB box is red, and amino acid D6, the first residue of the TonB box, is yellow. The figure illustrates the conformational motion that occurs in response to B12 binding: D6 flips over (A to D). The TonB box is within the barrel and does not extrude on ligand binding, and the TonB Cdomain is too large to enter the barrel.

Citation: Crosa J, Mey A, Payne S. 2004. Color Plates, In Iron Transport in Bacteria. ASM Press, Washington, DC.
Permissions and Reprints Request Permissions
Download as Powerpoint

This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error