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2wke

From Proteopedia

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Current revision

Crystal structure of the Actinomadura R39 DD-peptidase inhibited by 6- beta-iodopenicillanate.

Structural highlights

2wke is a 4 chain structure with sequence from Actinomadura sp. R39. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DAC_ACTSP Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

6-Beta-halogenopenicillanates are powerful, irreversible inhibitors of various beta-lactamases and penicillin-binding proteins. Upon acylation of these enzymes, the inhibitors are thought to undergo a structural rearrangement associated with the departure of the iodide and formation of a dihydrothiazine ring, but, to date, no structural evidence has proven this. 6-Beta-iodopenicillanic acid (BIP) is shown here to be an active antibiotic against various bacterial strains and an effective inhibitor of the class A beta-lactamase of Bacillus subtilis BS3 (BS3) and the D,D-peptidase of Actinomadura R39 (R39). Crystals of BS3 and of R39 were soaked with a solution of BIP and their structures solved at 1.65 and 2.2 A, respectively. The beta-lactam and the thiazolidine rings of BIP are indeed found to be fused into a dihydrothiazine ring that can adopt two stable conformations at these active sites. The rearranged BIP is observed in one conformation in the BS3 active site and in two monomers of the asymmetric unit of R39, and is observed in the other conformation in the other two monomers of the asymmetric unit of R39. The BS3 structure reveals a new mode of carboxylate interaction with a class A beta-lactamase active site that should be of interest in future inhibitor design.

Structural basis of the inhibition of class A beta-lactamases and penicillin-binding proteins by 6-beta-iodopenicillanate.,Sauvage E, Zervosen A, Dive G, Herman R, Amoroso A, Joris B, Fonze E, Pratt RF, Luxen A, Charlier P, Kerff F J Am Chem Soc. 2009 Oct 28;131(42):15262-9. PMID:19919161^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sauvage E, Zervosen A, Dive G, Herman R, Amoroso A, Joris B, Fonze E, Pratt RF, Luxen A, Charlier P, Kerff F. Structural basis of the inhibition of class A beta-lactamases and penicillin-binding proteins by 6-beta-iodopenicillanate. J Am Chem Soc. 2009 Oct 28;131(42):15262-9. PMID:19919161 doi:10.1021/ja9051526

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wke"

@@ Line 3: / Line 3: @@
 <StructureSection load='2wke' size='340' side='right'caption='[[2wke]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wke]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Actinomadura_sp. Actinomadura sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WKE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WKE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2wke]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinomadura_sp._R39 Actinomadura sp. R39]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WKE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WKE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BIY:(3S)-2,2-DIMETHYL-3,4-DIHYDRO-2H-1,4-THIAZINE-3,6-DICARBOXYLIC+ACID'>BIY</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w79|1w79]], [[1w8q|1w8q]], [[2vgj|2vgj]], [[2wix|2wix]], [[1w8y|1w8y]], [[2vgk|2vgk]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BIY:(3S)-2,2-DIMETHYL-3,4-DIHYDRO-2H-1,4-THIAZINE-3,6-DICARBOXYLIC+ACID'>BIY</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=2wke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wke OCA], [https://pdbe.org/2wke PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wke RCSB], [https://www.ebi.ac.uk/pdbsum/2wke PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wke ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2wke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wke OCA], [http://pdbe.org/2wke PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wke RCSB], [http://www.ebi.ac.uk/pdbsum/2wke PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wke ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DAC_ACTSP DAC_ACTSP]] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
+[https://www.uniprot.org/uniprot/DAC_ACTSP DAC_ACTSP] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 38: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Actinomadura sp]]
+[[Category: Actinomadura sp. R39]]
 [[Category: Large Structures]]
-[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
+[[Category: Charlier P]]
-[[Category: Charlier, P]]
+[[Category: Herman R]]
-[[Category: Herman, R]]
+[[Category: Kerff F]]
-[[Category: Kerff, F]]
+[[Category: Sauvage E]]
-[[Category: Sauvage, E]]
-[[Category: Actinomadura]]
-[[Category: Antibiotic resistance]]
-[[Category: Hydrolase]]
-[[Category: Iodopenicillanate]]
-[[Category: Penicillin binding]]

2wke

From Proteopedia

Current revision

Crystal structure of the Actinomadura R39 DD-peptidase inhibited by 6- beta-iodopenicillanate.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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