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[[Image:1hvb.gif|left|200px]]
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{{STRUCTURE_1hvb|  PDB=1hvb  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF STREPTOMYCES R61 DD-PEPTIDASE COMPLEXED WITH A NOVEL CEPHALOSPORIN ANALOG OF CELL WALL PEPTIDOGLYCAN'''


==CRYSTAL STRUCTURE OF STREPTOMYCES R61 DD-PEPTIDASE COMPLEXED WITH A NOVEL CEPHALOSPORIN ANALOG OF CELL WALL PEPTIDOGLYCAN==
<StructureSection load='1hvb' size='340' side='right'caption='[[1hvb]], [[Resolution|resolution]] 1.17&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hvb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._R61 Streptomyces sp. R61]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HVB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.17&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CEH:5-{3-(S)-(4-(R)-ACETYLAMINO-4-CARBOXY-BUTYRYLAMINO)-3-[1-(R)-(1-(R)-CARBOXY-ETHYLCARBAMOYL)-ETHYLCARBAMOYL]-PROPYL}-2-(CARBOXY-PHENYLACETYLAMINO-METHYL)-3,6-DIHYDRO-2H-[1,3]THIAZINE-4-CARBOXYLIC+ACID'>CEH</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hvb OCA], [https://pdbe.org/1hvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hvb RCSB], [https://www.ebi.ac.uk/pdbsum/1hvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hvb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DAC_STRSR DAC_STRSR] Catalyzes distinct carboxypeptidation and transpeptidation reactions during the last stages of wall peptidoglycan synthesis. Mistaking a beta-lactam antibiotic molecule for a normal substrate (i.e. a D-alanyl-D-alanine-terminated peptide), it becomes immobilized in the form of a long-lived, serine-ester-linked acyl enzyme and thus behave as penicillin-binding protein (PBP).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hv/1hvb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hvb ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:11171967</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1HVB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HVB OCA].
</div>
<div class="pdbe-citations 1hvb" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/11171967 11171967]
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Streptomyces sp.]]
__TOC__
[[Category: Kelly, J A.]]
</StructureSection>
[[Category: Lee, W.]]
[[Category: Large Structures]]
[[Category: McDonough, M A.]]
[[Category: Streptomyces sp. R61]]
[[Category: Mobashery, S.]]
[[Category: Kelly JA]]
[[Category: Silvaggi, N R.]]
[[Category: Lee W]]
[[Category: Protein-cephalosporin complex]]
[[Category: McDonough MA]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:16:10 2008''
[[Category: Mobashery S]]
[[Category: Silvaggi NR]]

Latest revision as of 06:43, 30 October 2024

CRYSTAL STRUCTURE OF STREPTOMYCES R61 DD-PEPTIDASE COMPLEXED WITH A NOVEL CEPHALOSPORIN ANALOG OF CELL WALL PEPTIDOGLYCAN

1hvb, resolution 1.17Å

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