Color Plates
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Editors:
Robert A. Bonomo1,
Marcelo E. Tolmasky2
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Affiliations:
1: Section of Infectious Diseases, Louis Stokes Cleveland Department of Veterans Affairs Medical Center, Cleveland, OH 44106;
2: Department of Biological Science, California State University-Fullerton, Fullerton, CA 92831
Content Type: Monograph
Publication Year:
2007
Category: Bacterial Pathogenesis
e-ISBN
:
9781555815615
Book DOI:
10.1128/9781555815615
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Figures
Color Plates
Citation:
Bonomo R, Tolmasky M.
2007.
Color Plates,
In
Enzyme-Mediated Resistance to Antibiotics.
ASM Press, Washington, DC.
/content/10.1128/9781555815615.app01.f0ps1-01.jpg
COLOR PLATE 1 (chapter 7)
Structures of PBPs. Ribbon diagrams showing the structures of E. faecium PBP5 (type B1) (a) and S. pneumoniae PBP2x (type B4) (b).
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Click to view
COLOR PLATE 1 (chapter 7)
Structures of PBPs. Ribbon diagrams showing the structures of E. faecium PBP5 (type B1) (a) and S. pneumoniae PBP2x (type B4) (b).
Citation:
Bonomo R, Tolmasky M.
2007.
Color Plates,
In
Enzyme-Mediated Resistance to Antibiotics.
ASM Press, Washington, DC.
/content/10.1128/9781555815615.app01.f0ps2-01.jpg
COLOR PLATE 2 (chapter 7)
Structure of the active site of S. aureus PBP2’ acyl enzyme complex with nitrocefin. The structure (78) is shown as ball and stick model with the protein overlaid by an electrostatic surface calculated using MOLOC.
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COLOR PLATE 2 (chapter 7)
Structure of the active site of S. aureus PBP2’ acyl enzyme complex with nitrocefin. The structure (78) is shown as ball and stick model with the protein overlaid by an electrostatic surface calculated using MOLOC.
Citation:
Bonomo R, Tolmasky M.
2007.
Color Plates,
In
Enzyme-Mediated Resistance to Antibiotics.
ASM Press, Washington, DC.
/content/10.1128/9781555815615.app01.f0ps2-02.jpg
COLOR PLATE 3 (chapter 7)
Location of point mutations of E. faecium PBP5 conferring β-lactam resistance. The alpha-carbon chain of the structure of the transpeptidase domain of the acyl enzyme complex (120) formed with benzylpenicillin is shown with the inhibitor and the side chains of the residues implicated in β-lactam resistance shown as ball and stick models.
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COLOR PLATE 3 (chapter 7)
Location of point mutations of E. faecium PBP5 conferring β-lactam resistance. The alpha-carbon chain of the structure of the transpeptidase domain of the acyl enzyme complex (120) formed with benzylpenicillin is shown with the inhibitor and the side chains of the residues implicated in β-lactam resistance shown as ball and stick models.
Citation:
Bonomo R, Tolmasky M.
2007.
Color Plates,
In
Enzyme-Mediated Resistance to Antibiotics.
ASM Press, Washington, DC.
/content/10.1128/9781555815615.app01.f0ps3-01.jpg
COLOR PLATE 4 (chapter 11)
Folding of OXA-10 protein (1FOF) as a ribbon presentation, with OXA-10 numbering. Key residues in the active site and the omega loop are indicated.
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COLOR PLATE 4 (chapter 11)
Folding of OXA-10 protein (1FOF) as a ribbon presentation, with OXA-10 numbering. Key residues in the active site and the omega loop are indicated.
Citation:
Bonomo R, Tolmasky M.
2007.
Color Plates,
In
Enzyme-Mediated Resistance to Antibiotics.
ASM Press, Washington, DC.
/content/10.1128/9781555815615.app01.f0ps3-02.jpg
COLOR PLATE 5 (chapter 11)
Conserved residues in OXA-10 (1FOF) (67Ser-Xxx-Xxx-Lys, 115Ser-Xxx-Val, and 205Lys-Xxx-Gly [OXA-10 numbering]).
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COLOR PLATE 5 (chapter 11)
Conserved residues in OXA-10 (1FOF) (67Ser-Xxx-Xxx-Lys, 115Ser-Xxx-Val, and 205Lys-Xxx-Gly [OXA-10 numbering]).
Citation:
Bonomo R, Tolmasky M.
2007.
Color Plates,
In
Enzyme-Mediated Resistance to Antibiotics.
ASM Press, Washington, DC.
/content/10.1128/9781555815615.app01.f0ps4-01.jpg
COLOR PLATE 6 (chapter 11)
OXA-13 β-lactamase, acylated by meropenem. The structure is a closed form with a noncarboxylated lysine. A water molecule (the big ball) is positioned at the end of Lys73 (70 in OXA-13) at a position similar to that of the carboxylate, and is correctly positioned to be catalytic. Strong hydrogen bonds are represented as dashed lines. Residues are numbered using OXA-10 numbering.
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COLOR PLATE 6 (chapter 11)
OXA-13 β-lactamase, acylated by meropenem. The structure is a closed form with a noncarboxylated lysine. A water molecule (the big ball) is positioned at the end of Lys73 (70 in OXA-13) at a position similar to that of the carboxylate, and is correctly positioned to be catalytic. Strong hydrogen bonds are represented as dashed lines. Residues are numbered using OXA-10 numbering.
Citation:
Bonomo R, Tolmasky M.
2007.
Color Plates,
In
Enzyme-Mediated Resistance to Antibiotics.
ASM Press, Washington, DC.
/content/10.1128/9781555815615.app01.f0ps4-02.jpg
COLOR PLATE 7 (chapter 13)
X-ray crystal structure of ZipA (space-filling depiction in both panels) interacting with the carboxy-terminal peptide of FtsZ (ball and stick on left and space filling on right).
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10.1128/9781555815615/f0ps4-02.gif
Click to view
COLOR PLATE 7 (chapter 13)
X-ray crystal structure of ZipA (space-filling depiction in both panels) interacting with the carboxy-terminal peptide of FtsZ (ball and stick on left and space filling on right).
Citation:
Bonomo R, Tolmasky M.
2007.
Color Plates,
In
Enzyme-Mediated Resistance to Antibiotics.
ASM Press, Washington, DC.
/content/10.1128/9781555815615.app01.f0ps5-01.jpg
COLOR PLATE 8 (chapter 15)
Three-dimensional structure of EmrE from E. coli (Protein Data Bank [PDB] code 2f2m). Monomers are represented as green and blue ribbons. A bound TPP molecule is shown in red, and black lines indicate a proposed position of the lipid bilayer.
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COLOR PLATE 8 (chapter 15)
Three-dimensional structure of EmrE from E. coli (Protein Data Bank [PDB] code 2f2m). Monomers are represented as green and blue ribbons. A bound TPP molecule is shown in red, and black lines indicate a proposed position of the lipid bilayer.
Citation:
Bonomo R, Tolmasky M.
2007.
Color Plates,
In
Enzyme-Mediated Resistance to Antibiotics.
ASM Press, Washington, DC.
/content/10.1128/9781555815615.app01.f0ps5-02.jpg
COLOR PLATE 9 (chapter 15)
(A) Three-dimensional structure of AcrB from .E. coli (Protein Data Bank [PDB] code 1iwg). Monomers are shown as red, blue, and green ribbons. Black lines indicate the approximate position of the inner membrane. (B) Top view of an AcrB trimer as seen from the periplasmic side.
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COLOR PLATE 9 (chapter 15)
(A) Three-dimensional structure of AcrB from .E. coli (Protein Data Bank [PDB] code 1iwg). Monomers are shown as red, blue, and green ribbons. Black lines indicate the approximate position of the inner membrane. (B) Top view of an AcrB trimer as seen from the periplasmic side.
Citation:
Bonomo R, Tolmasky M.
2007.
Color Plates,
In
Enzyme-Mediated Resistance to Antibiotics.
ASM Press, Washington, DC.
/content/10.1128/9781555815615.app01.f0ps6-01.jpg
COLOR PLATE 10 (chapter 15)
(A) Three-dimensional structure of TolC from E. coli (Protein Data Base [PDB] code 1ek9). Monomers are shown as red, blue, and green ribbons. Black lines indicate the approximate position of the outer membrane. (B) Bottom view of a TolC trimer as seen from the periplasmic side.
10.1128/9781555815615/f0ps6-01_thmb.gif
10.1128/9781555815615/f0ps6-01.gif
Click to view
COLOR PLATE 10 (chapter 15)
(A) Three-dimensional structure of TolC from E. coli (Protein Data Base [PDB] code 1ek9). Monomers are shown as red, blue, and green ribbons. Black lines indicate the approximate position of the outer membrane. (B) Bottom view of a TolC trimer as seen from the periplasmic side.
Citation:
Bonomo R, Tolmasky M.
2007.
Color Plates,
In
Enzyme-Mediated Resistance to Antibiotics.
ASM Press, Washington, DC.
/content/10.1128/9781555815615.app01.f0ps7-01.jpg
COLOR PLATE 11 (chapter 20)
Structure of the class 1 integrase complex with DNA (Protein Data Bank).
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COLOR PLATE 11 (chapter 20)
Structure of the class 1 integrase complex with DNA (Protein Data Bank).
Citation:
Bonomo R, Tolmasky M.
2007.
Color Plates,
In
Enzyme-Mediated Resistance to Antibiotics.
ASM Press, Washington, DC.
/content/10.1128/9781555815615.app01.f0ps8-01.jpg
COLOR PLATE 12 (chapter 20)
Binding of the integrase to DNA. From MacDonald et al. (8).
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Click to view
COLOR PLATE 12 (chapter 20)
Binding of the integrase to DNA. From MacDonald et al. (8).
Citation:
Bonomo R, Tolmasky M.
2007.
Color Plates,
In
Enzyme-Mediated Resistance to Antibiotics.
ASM Press, Washington, DC.
/content/10.1128/9781555815615.app01.f0ps8-02.jpg
COLOR PLATE 13 (chapter 20)
Proposed IntI excision through a single-stranded DNA substrate pathway based upon a previously proposed model by Mazen et al. The bottom strand of the integron element, produced by conjugation or transformation, folds upon itself to yield an active stem-loop substrate (step 1). Two IntI molecules bind each folded attC site to form an antiparallel recombination synapse (step 2). Here, the HJ intermediate requires cellular components in order to be resolved (steps 5 and 6). IntI molecules colored green or magenta are potentially active or nonactive for cleavage, respectively.
10.1128/9781555815615/f0ps8-02_thmb.gif
10.1128/9781555815615/f0ps8-02.gif
Click to view
COLOR PLATE 13 (chapter 20)
Proposed IntI excision through a single-stranded DNA substrate pathway based upon a previously proposed model by Mazen et al. The bottom strand of the integron element, produced by conjugation or transformation, folds upon itself to yield an active stem-loop substrate (step 1). Two IntI molecules bind each folded attC site to form an antiparallel recombination synapse (step 2). Here, the HJ intermediate requires cellular components in order to be resolved (steps 5 and 6). IntI molecules colored green or magenta are potentially active or nonactive for cleavage, respectively.
Citation:
Bonomo R, Tolmasky M.
2007.
Color Plates,
In
Enzyme-Mediated Resistance to Antibiotics.
ASM Press, Washington, DC.
/content/book/10.1128/9781555815615.app01
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