1hvb
From Proteopedia
(New page: 200px<br /><applet load="1hvb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hvb, resolution 1.17Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1hvb.gif|left|200px]]<br /><applet load="1hvb" size=" | + | [[Image:1hvb.gif|left|200px]]<br /><applet load="1hvb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hvb, resolution 1.17Å" /> | caption="1hvb, resolution 1.17Å" /> | ||
'''CRYSTAL STRUCTURE OF STREPTOMYCES R61 DD-PEPTIDASE COMPLEXED WITH A NOVEL CEPHALOSPORIN ANALOG OF CELL WALL PEPTIDOGLYCAN'''<br /> | '''CRYSTAL STRUCTURE OF STREPTOMYCES R61 DD-PEPTIDASE COMPLEXED WITH A NOVEL CEPHALOSPORIN ANALOG OF CELL WALL PEPTIDOGLYCAN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The cell wall imparts structural strength and shape to bacteria. It is | + | The cell wall imparts structural strength and shape to bacteria. It is made up of polymeric glycan chains with peptide branches that are cross-linked to form the cell wall. The cross-linking reaction, catalyzed by transpeptidases, is the last step in cell wall biosynthesis. These enzymes are members of the family of penicillin-binding proteins, the targets of beta-lactam antibiotics. We report herein the structure of a penicillin-binding protein complexed with a cephalosporin designed to probe the mechanism of the cross-linking reaction catalyzed by transpeptidases. The 1.2-A resolution x-ray structure of this cephalosporin bound to the active site of the bifunctional serine type D-alanyl-D-alanine carboxypeptidase/transpeptidase (EC ) from Streptomyces sp. strain R61 reveals how the two peptide strands from the polymeric substrates are sequestered in the active site of a transpeptidase. The structure of this complex provides a snapshot of the enzyme and the bound cell wall components poised for the final and critical cross-linking step of cell wall biosynthesis. |
==About this Structure== | ==About this Structure== | ||
| - | 1HVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.] with CEH as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4] Full crystallographic information is available from [http:// | + | 1HVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.] with <scene name='pdbligand=CEH:'>CEH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HVB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces sp.]] | [[Category: Streptomyces sp.]] | ||
| - | [[Category: Kelly, J | + | [[Category: Kelly, J A.]] |
[[Category: Lee, W.]] | [[Category: Lee, W.]] | ||
| - | [[Category: McDonough, M | + | [[Category: McDonough, M A.]] |
[[Category: Mobashery, S.]] | [[Category: Mobashery, S.]] | ||
| - | [[Category: Silvaggi, N | + | [[Category: Silvaggi, N R.]] |
[[Category: CEH]] | [[Category: CEH]] | ||
[[Category: protein-cephalosporin complex]] | [[Category: protein-cephalosporin complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:14 2008'' |
Revision as of 11:05, 21 February 2008
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CRYSTAL STRUCTURE OF STREPTOMYCES R61 DD-PEPTIDASE COMPLEXED WITH A NOVEL CEPHALOSPORIN ANALOG OF CELL WALL PEPTIDOGLYCAN
Overview
The cell wall imparts structural strength and shape to bacteria. It is made up of polymeric glycan chains with peptide branches that are cross-linked to form the cell wall. The cross-linking reaction, catalyzed by transpeptidases, is the last step in cell wall biosynthesis. These enzymes are members of the family of penicillin-binding proteins, the targets of beta-lactam antibiotics. We report herein the structure of a penicillin-binding protein complexed with a cephalosporin designed to probe the mechanism of the cross-linking reaction catalyzed by transpeptidases. The 1.2-A resolution x-ray structure of this cephalosporin bound to the active site of the bifunctional serine type D-alanyl-D-alanine carboxypeptidase/transpeptidase (EC ) from Streptomyces sp. strain R61 reveals how the two peptide strands from the polymeric substrates are sequestered in the active site of a transpeptidase. The structure of this complex provides a snapshot of the enzyme and the bound cell wall components poised for the final and critical cross-linking step of cell wall biosynthesis.
About this Structure
1HVB is a Single protein structure of sequence from Streptomyces sp. with as ligand. Active as Serine-type D-Ala-D-Ala carboxypeptidase, with EC number 3.4.16.4 Full crystallographic information is available from OCA.
Reference
A 1.2-A snapshot of the final step of bacterial cell wall biosynthesis., Lee W, McDonough MA, Kotra L, Li ZH, Silvaggi NR, Takeda Y, Kelly JA, Mobashery S, Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1427-31. PMID:11171967
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