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[[Image:1yqs.gif|left|200px]]
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{{STRUCTURE_1yqs|  PDB=1yqs  |  SCENE=  }}
'''Inhibition of the R61 DD-Peptidase by N-benzoyl-beta-sultam'''


==Inhibition of the R61 DD-Peptidase by N-benzoyl-beta-sultam==
<StructureSection load='1yqs' size='340' side='right'caption='[[1yqs]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</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/yq/1yqs_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=1yqs ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1YQS 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=1YQS OCA].
</div>
<div class="pdbe-citations 1yqs" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/15909988 15909988]
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Streptomyces sp.]]
__TOC__
[[Category: Ahmed, N.]]
</StructureSection>
[[Category: Cordaro, M.]]
[[Category: Large Structures]]
[[Category: Delmarcelle, M.]]
[[Category: Streptomyces sp. R61]]
[[Category: Kelly, J A.]]
[[Category: Ahmed N]]
[[Category: Laws, A P.]]
[[Category: Cordaro M]]
[[Category: Page, M I.]]
[[Category: Delmarcelle M]]
[[Category: Silvaggi, N R.]]
[[Category: Kelly JA]]
[[Category: Beta-lactam]]
[[Category: Laws AP]]
[[Category: Beta-sultam]]
[[Category: Page MI]]
[[Category: Cell well biosynthesis]]
[[Category: Silvaggi NR]]
[[Category: Peptidase]]
[[Category: Sulfonylation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:39:53 2008''

Latest revision as of 07:42, 30 October 2024

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

1yqs, resolution 1.05Å

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