1yqs

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{{Seed}}
 
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[[Image:1yqs.png|left|200px]]
 
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==Inhibition of the R61 DD-Peptidase by N-benzoyl-beta-sultam==
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The line below this paragraph, containing "STRUCTURE_1yqs", creates the "Structure Box" on the page.
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<StructureSection load='1yqs' size='340' side='right'caption='[[1yqs]], [[Resolution|resolution]] 1.05&Aring;' 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'>[[1yqs]] 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=1YQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YQS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.05&#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=BSA:2-(BENZOYLAMINO)ETHANESULFONIC+ACID'>BSA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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{{STRUCTURE_1yqs| PDB=1yqs | SCENE= }}
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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=1yqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqs OCA], [https://pdbe.org/1yqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yqs RCSB], [https://www.ebi.ac.uk/pdbsum/1yqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yqs 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/yq/1yqs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1yqs 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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N-Acyl-beta-sultams are time-dependent, irreversible active site-directed inhibitors of Streptomyces R61 DD-peptidase. The rate of inactivation is first order with respect to beta-sultam concentration, and the second-order rate constants show a dependence on pH similar to that for the hydrolysis of a substrate. Inactivation is due to the formation of a stable 1:1 enzyme-inhibitor complex as a result of the active site serine being sulfonylated by the beta-sultam as shown by ESI-MS analysis and by X-ray crystallography. A striking feature of the sulfonyl enzyme is that the inhibitor is not bound to the oxyanion hole but interacts extensively with the "roof" of the active site where the Arg 285 is located.
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===Inhibition of the R61 DD-Peptidase by N-benzoyl-beta-sultam===
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Inactivation of bacterial DD-peptidase by beta-sultams.,Llinas A, Ahmed N, Cordaro M, Laws AP, Frere JM, Delmarcelle M, Silvaggi NR, Kelly JA, Page MI Biochemistry. 2005 May 31;44(21):7738-46. PMID:15909988<ref>PMID:15909988</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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</div>
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<div class="pdbe-citations 1yqs" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15909988}}, adds the Publication Abstract to the page
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*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15909988 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15909988}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1YQS is a 1 chain 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=1YQS OCA].
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[[Category: Streptomyces sp. R61]]
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[[Category: Ahmed N]]
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==Reference==
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[[Category: Cordaro M]]
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<ref group="xtra">PMID:15909988</ref><references group="xtra"/>
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[[Category: Delmarcelle M]]
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[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
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[[Category: Kelly JA]]
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[[Category: Streptomyces sp.]]
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[[Category: Laws AP]]
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[[Category: Ahmed, N.]]
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[[Category: Page MI]]
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[[Category: Cordaro, M.]]
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[[Category: Silvaggi NR]]
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[[Category: Delmarcelle, M.]]
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[[Category: Kelly, J A.]]
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[[Category: Laws, A P.]]
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[[Category: Page, M I.]]
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[[Category: Silvaggi, N R.]]
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[[Category: Beta-lactam]]
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[[Category: Beta-sultam]]
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[[Category: Cell well biosynthesis]]
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[[Category: Peptidase]]
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[[Category: Sulfonylation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:53:45 2009''
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Current revision

Inhibition of the R61 DD-Peptidase by N-benzoyl-beta-sultam

PDB ID 1yqs

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