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Color Plates

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Image of Color Plate 3.1

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Color Plate 3.1

A general view of how the specific immune system defends the body against an antigen from a bacterium. Reprinted from Sci. Am., special issue, September 1993, with permission from Carol Donner.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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Image of Color Plate 12.1

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Color Plate 12.1

Ribbon diagram of TEM-1 β-lactamaseshowing the positions of amino acid substitutions found inESBLs. The substitutions that result in increased hydrolysis ofthe extended-spectrum cephalosporins cefotaxime and ceftazidimeare shown in blue. The positions where substitutionsdecrease the affinity of the enzyme for inhibitors are shown ingreen. The positions where amino acid substitutions havebeen identified that do not affect the catalytic activity of theenzyme are shown in magenta. Reprinted from T. Patzkill, ASMNews 64:90–95, 1998, with permission from the AmericanSociety for Microbiology.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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Image of Color Plate 16.1

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Color Plate 16.1

Three-dimensional structure of yeast tRNAPhe deduced from X-ray diffractionanalysis. The shape resembles a twisted L. (a) Schematic diagram with the variousarms identified. (b) Space-filling model. Color coding is the same in both representations.The three bases of the anticodon are shown in red, and the CCA sequence at the 3′ end isshown in orange. The TψC and D arms are blue and yellow, respectively. Reprinted fromD. L. Nelson and M. M. Cox, Lehninger Principles of Biochemistry, 4th ed. (Worth Publishers,New York, N.Y., 2000), with permission from the publisher.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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Image of >Color Plate 16.2

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>Color Plate 16.2

Steps in the formation of the prokaryotic 70S initiation complex. Reprinted from H. R. Horton, L. A. Moran, R. S. Ochs, J. D. Rawn, and K. G. Scrimgeour, Principles of Biochemistry, 3rd ed. (Prentice-Hall, Upper Saddle River, N.J., 2002), with permission from the publisher.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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Image of >Color Plate 16.3

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>Color Plate 16.3

Insertion of aminoacyl-tRNAinto the A site by GTP–EF-Tu during the chainelongation step in E. coli. Reprinted from H. R.Horton, L. A. Moran, R. S. Ochs, J. D. Rawn, andK. G. Scrimgeour, Principles of Biochemistry, 3rd ed. (Prentice-Hall, Upper Saddle River, N.J.,2002), with permission from the publisher.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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Image of Color Plate 16.4

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Color Plate 16.4

Cycling of EF-Tu–GTP. Reprinted from H. R. Horton, L. A. Moran, R. S. Ochs, J. D. Rawn, and K. G. Scrimgeour, Principles of Biochemistry, 3rd ed. (Prentice-Hall, Upper Saddle River, N.J., 2002), with permission from the publisher.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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Image of Color Plate 16.5

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Color Plate 16.5

Translocation during proteinsynthesis in prokaryotes. Reprinted fromH. R. Horton, L. A. Moran, R. S. Ochs, J. D.Rawn, and K. G. Scrimgeour, Principles of Biochemistry, 3rd ed. (Prentice-Hall, Upper Saddle River, N.J., 2002), with permission from the publisher.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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Image of Color Plate 16.6a

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Color Plate 16.6a

Secondary and tertiarystructures of 16S, 23S, and 5S rRNA. (A) Secondarystructure of T. thermophilus 16S rRNA.(B) Secondary structures of T. thermophilus23S and 5S rRNA. (C) Three-dimensional foldof 16S rRNA in the 70S ribosome. (D) Threedimensionalfold of 23S and 5S rRNA. Reprintedfrom M. M. Yusupov, G. Z. Yusupova, A. Baucom,K. Lieberman, T. N. Earnest, J. H. Cate, andH. F. Noller, Science 292:883–896, 2001, withpermission from the publisher.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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Image of Color Plate 16.6b

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Color Plate 16.6b

Secondary and tertiarystructures of 16S, 23S, and 5S rRNA. (A) Secondarystructure of T. thermophilus 16S rRNA.(B) Secondary structures of T. thermophilus23S and 5S rRNA. (C) Three-dimensional foldof 16S rRNA in the 70S ribosome. (D) Threedimensionalfold of 23S and 5S rRNA. Reprintedfrom M. M. Yusupov, G. Z. Yusupova, A. Baucom,K. Lieberman, T. N. Earnest, J. H. Cate, andH. F. Noller, Science 292:883–896, 2001, withpermission from the publisher.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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Image of Color Plate 22.1

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Color Plate 22.1

Structure of T. aquaticus RNA polymerasecore enzyme. Reprinted from H. R. Horton, L. A. Moran, R. S.Ochs, J. D. Rawn, and K. G. Scrimgeour, Principles of Biochemistry,3rd ed. (Prentice-Hall, Upper Saddle River, N.J., 2002), withpermission from the publisher.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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Image of >Color Plate 22.2

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>Color Plate 22.2

Transcription by RNA polymerase in E. coli. To synthesize an RNAstrand complementary to one of the two DNA strands in a double helix, the DNA is transientlyunwound. (a) About 17 bp is unwound at any given time. The transcription bubblemoves from left to right as shown, keeping pace with RNA synthesis. The DNA isunwound ahead and rewound behind as RNA is transcribed. Red arrows show the directionin which the DNA and the short RNA-DNA hybrid must rotate to permit this process.(b) Supercoiling of DNA brought about by transcription. Positive supercoils form ahead ofthe transcription bubble, and negative supercoils form behind. Reprinted from D. L. Nelsonand M. M. Cox, Lehninger Principles of Biochemistry, 3rd ed. (Worth Publishers, NewYork, N.Y., 2000), with permission from the publisher.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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Image of Color Plate 27.1

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Color Plate 27.1

Ribbon diagram of the E. coli deformylaseviewed toward the substrate cleft into the metal center.The secondary structure is color coded with α-helical regionsas blue, β-sheet regions as red, and the remainder as green.The metal cation is shown as green. Reprinted from M. K.Chan, W. Gong, P. T. Ravi Rajagopalan, B. Hao, C. M. Tsai,and D. Pei, Biochemistry 36:13904–13909, 1997, with permissionfrom the publisher.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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Image of Color Plate A1

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Color Plate A1

The tertiary structure describes the shape ofthe fully folded polypeptide chain. The example shown is theinhibitor barbituric acid ribonucleotide bound in the active siteof orotidine 5′-monophosphate decarboxylase. The enzyme iscomposed of β-strands and α-helices. Reprinted from K. N.Houk et al., ChemBioChem 2:113–118, 2001, with permissionfrom the publisher.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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Color Plate A2

Ribbon diagram of the C2 backbone of HIV-1 protease. Reprinted from E. De Clercq, J. Med. Chem. 38:2491–2517, 1995, with permission from the publisher.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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Image of >Color Plate D1

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>Color Plate D1

Ribbon diagram of FepA. The extracellularspace is located at the top of the illustration,and the periplasmic space is at the bottom. The putativeiron position of ferric enterobactin is indicated bythe red sphere. Part of the barrel has been renderedtransparent to reveal the N-terminal domain located inthe channel. Reprinted from S. K. Buchanan, B. S.Smith, L. Venkatramani, D. Xia, L. Esser, M. Palnitker, R.Chakraborty, D. van der Helm, and J. Deisenhofer, Nat.Struct. Biol. 6:56–63, 1999, with permission from thepublisher.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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Image of Color Plate D2

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Color Plate D2

Ribbon diagram of the crystal structureof TolC. A trimeric TolC molecule forms the combinedβ-barrel/α-helical “tunnel” structure. Eachmonomer is shown in a different color. Reprinted from V.Koronakis, A. Sharif, E. Koronakis, B. Luisi, and C. Hughes,Nature 405:914–919, 2000, with permission from thepublisher.

Citation: Mascaretti O. 2003. Color Plates, In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC.
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