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1hvb

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(New page: 200px<br /><applet load="1hvb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hvb, resolution 1.17&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1hvb.gif|left|200px]]<br /><applet load="1hvb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hvb, resolution 1.17&Aring;" />
 
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'''CRYSTAL STRUCTURE OF STREPTOMYCES R61 DD-PEPTIDASE COMPLEXED WITH A NOVEL CEPHALOSPORIN ANALOG OF CELL WALL PEPTIDOGLYCAN'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF STREPTOMYCES R61 DD-PEPTIDASE COMPLEXED WITH A NOVEL CEPHALOSPORIN ANALOG OF CELL WALL PEPTIDOGLYCAN==
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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.
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<StructureSection load='1hvb' size='340' side='right'caption='[[1hvb]], [[Resolution|resolution]] 1.17&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hv/1hvb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HVB OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11171967 11171967]
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</div>
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[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
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<div class="pdbe-citations 1hvb" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Streptomyces sp.]]
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[[Category: Kelly, J.A.]]
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[[Category: Lee, W.]]
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[[Category: McDonough, M.A.]]
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[[Category: Mobashery, S.]]
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[[Category: Silvaggi, N.R.]]
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[[Category: CEH]]
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[[Category: protein-cephalosporin complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:51:16 2007''
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==See Also==
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*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Streptomyces sp. R61]]
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[[Category: Kelly JA]]
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[[Category: Lee W]]
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[[Category: McDonough MA]]
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[[Category: Mobashery S]]
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[[Category: Silvaggi NR]]

Current revision

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

PDB ID 1hvb

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