5ggw: Difference between revisions

Revision as of 11:31, 2 August 2023

Crystal structure of Class C beta-lactamase

Structural highlights

5ggw is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.762Å
Ligands:	PO4, SO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B7SNP8_ECOLX

Publication Abstract from PubMed

AmpC BER is an extended substrate spectrum class C beta-lactamase with a two-amino-acid insertion in the R2 loop compared with AmpC EC2. The crystal structures of AmpC BER (S64A mutant) and AmpC EC2 were determined. Structural comparison of the two proteins revealed that the insertion increases the conformational flexibility of the R2 loop. Two citrate molecules originating from the crystallization solution were observed in the active site of the S64A mutant. One citrate molecule makes extensive interactions with active-site residues that are highly conserved among class C beta-lactamases, whereas the other one is weakly bound. Based on this structural observation, it is demonstrated that citrate, a primary metabolite that is widely used as a food additive, is a competitive inhibitor of two class C beta-lactamases (AmpC BER and CMY-10). Consequently, the data indicate enhancement of the flexibility of the R2 loop as an operative strategy for molecular evolution of extended-spectrum class C beta-lactamases, and also suggest that the citrate scaffold is recognized by the active sites of class C beta-lactamases.

Structural basis for the extended substrate spectrum of AmpC BER and structure-guided discovery of the inhibition activity of citrate against the class C beta-lactamases AmpC BER and CMY-10.,Na JH, Cha SS Acta Crystallogr D Struct Biol. 2016 Aug;72(Pt 8):976-85. doi:, 10.1107/S2059798316011311. Epub 2016 Jul 28. PMID:27487828^[1]

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

References

↑ Na JH, Cha SS. Structural basis for the extended substrate spectrum of AmpC BER and structure-guided discovery of the inhibition activity of citrate against the class C beta-lactamases AmpC BER and CMY-10. Acta Crystallogr D Struct Biol. 2016 Aug;72(Pt 8):976-85. doi:, 10.1107/S2059798316011311. Epub 2016 Jul 28. PMID:27487828 doi:https://dx.doi.org/10.1107/S2059798316011311

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Na JH, Cha SS. Structural basis for the extended substrate spectrum of AmpC BER and structure-guided discovery of the inhibition activity of citrate against the class C beta-lactamases AmpC BER and CMY-10. Acta Crystallogr D Struct Biol. 2016 Aug;72(Pt 8):976-85. doi:, 10.1107/S2059798316011311. Epub 2016 Jul 28. PMID:27487828 doi:https://dx.doi.org/10.1107/S2059798316011311

[1]

@@ Line 3: / Line 3: @@
 <StructureSection load='5ggw' size='340' side='right'caption='[[5ggw]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ggw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GGW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GGW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ggw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GGW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.762&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ampC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </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=5ggw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ggw OCA], [https://pdbe.org/5ggw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ggw RCSB], [https://www.ebi.ac.uk/pdbsum/5ggw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ggw 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=5ggw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ggw OCA], [http://pdbe.org/5ggw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ggw RCSB], [http://www.ebi.ac.uk/pdbsum/5ggw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ggw ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/B7SNP8_ECOLX B7SNP8_ECOLX]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 25: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: Beta-lactamase]]
 [[Category: Large Structures]]
-[[Category: An, Y J]]
+[[Category: An YJ]]
-[[Category: Cha, S S]]
+[[Category: Cha SS]]
-[[Category: Na, J H]]
+[[Category: Na JH]]
-[[Category: Class c]]
-[[Category: Hydrolase]]

5ggw: Difference between revisions

Revision as of 11:31, 2 August 2023

Crystal structure of Class C beta-lactamase

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools