1van

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[[Image:1van.png|left|200px]]
 
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==DIFFERENT MODES OF VANCOMYCIN AND D-ALANYL-D-ALANINE PEPTIDASE BINDING TO CELL WALL PEPTIDE AND A POSSIBLE ROLE FOR THE VANCOMYCIN RESISTANCE PROTEIN==
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The line below this paragraph, containing "STRUCTURE_1van", creates the "Structure Box" on the page.
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<StructureSection load='1van' size='340' side='right'caption='[[1van]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VAN FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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=1van FirstGlance], [https://www.ebi.ac.uk/pdbsum/1van PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1van ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1van| PDB=1van | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A comparison was made of the binding modes of the bacterial cell wall precursor L-lysyl-D-alanyl-D-alanine to the glycopeptide antibiotic vancomycin and to the D-alanyl-D-alanine-cleaving peptidase of Streptomyces sp. strain R61, a model for cell wall-synthesizing enzymes whose X-ray three-dimensional structure is established. In each of the two pairings (vancomycin with peptide and DD-peptidase with peptide), polypeptide backbones were antiparallel, and the antibiotic or enzyme enveloped the peptide substrate from opposite sides. Hydrogen-bonding groups on the substrate which are involved with the DD-peptidase were shown to be different from the ones reported from nuclear magnetic resonance studies to be involved with vancomycin. Because of steric hindrance, the binding of either molecule to the substrate prevents the binding of the other molecule. Binding to the substrate by a D-alanyl-D-alanine-recognizing protein in a manner similar to that used by the DD-peptidase could explain recent observations of vancomycin resistance, in which a new membrane-associated protein has been detected.
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===DIFFERENT MODES OF VANCOMYCIN AND D-ALANYL-D-ALANINE PEPTIDASE BINDING TO CELL WALL PEPTIDE AND A POSSIBLE ROLE FOR THE VANCOMYCIN RESISTANCE PROTEIN===
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Different modes of vancomycin and D-alanyl-D-alanine peptidase binding to cell wall peptide and a possible role for the vancomycin resistance protein.,Knox JR, Pratt RF Antimicrob Agents Chemother. 1990 Jul;34(7):1342-7. PMID:2386365<ref>PMID:2386365</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_2386365}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1van" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 2386365 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_2386365}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VAN OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:2386365</ref><references group="xtra"/>
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[[Category: Knox, J R]]
[[Category: Knox, J R]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 08:47:31 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

DIFFERENT MODES OF VANCOMYCIN AND D-ALANYL-D-ALANINE PEPTIDASE BINDING TO CELL WALL PEPTIDE AND A POSSIBLE ROLE FOR THE VANCOMYCIN RESISTANCE PROTEIN

PDB ID 1van

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