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3q6v

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<StructureSection load='3q6v' size='340' side='right'caption='[[3q6v]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
<StructureSection load='3q6v' size='340' side='right'caption='[[3q6v]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3q6v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29844 Atcc 29844]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q6V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q6V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3q6v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_fonticola Serratia fonticola]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q6V FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 1.37&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3q42|3q42]]</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blaSfh-I, sfhI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=47917 ATCC 29844])</td></tr>
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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=3q6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q6v OCA], [https://pdbe.org/3q6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q6v RCSB], [https://www.ebi.ac.uk/pdbsum/3q6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q6v ProSAT]</span></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3q6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q6v OCA], [http://pdbe.org/3q6v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3q6v RCSB], [http://www.ebi.ac.uk/pdbsum/3q6v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3q6v ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9RMI1_SERFO Q9RMI1_SERFO]
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Metallo-beta-lactamases (MBLs) or class B beta-lactamases are zinc-dependent enzymes capable of inactivating almost all classes of beta-lactam antibiotics. To date, no MBL inhibitors are available for clinical use. Of the three MBL subclasses, B2 enzymes, unlike those from subclasses B1 and B3, are fully active with one zinc ion bound and possess a narrow spectrum of activity, hydrolyzing carbapenem substrates almost exclusively. These remain the least studied MBLs. Sfh-I, originally identified from the aquatic bacterium Serratia fonticola UTAD54, is a divergent member of this group. Previous B2 MBL structures, available only for the CphA enzyme from Aeromonas hydrophila, all contain small molecules bound in their active sites. In consequence, the mechanism by which these enzymes activate the water nucleophile required for beta-lactam hydrolysis remains to be unambiguously established. Here we report crystal structures of Sfh-I as a complex with glycerol and in the unliganded form, revealing for the first time the disposition of water molecules in the B2 MBL active site. Our data indicate that the hydrolytic water molecule is activated by His118 rather than by Asp120 and/or zinc. Consistent with this proposal, we show that the environment of His118 in B2 MBLs is distinct from that of the B1 and B3 enzymes, where this residue acts as a zinc ligand, and offer a structure-based mechanism for beta-lactam hydrolysis by these enzymes.
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Crystal structure of Serratia fonticola Sfh-I: activation of the nucleophile in mono-zinc metallo-beta-lactamases.,Fonseca F, Bromley EH, Saavedra MJ, Correia A, Spencer J J Mol Biol. 2011 Sep 2;411(5):951-9. Epub 2011 Jul 6. PMID:21762699<ref>PMID:21762699</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 3q6v" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 29844]]
 
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[[Category: Beta-lactamase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Correia, A]]
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[[Category: Serratia fonticola]]
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[[Category: Fonseca, F]]
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[[Category: Correia A]]
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[[Category: Saavedra, M J]]
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[[Category: Fonseca F]]
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[[Category: Spencer, J]]
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[[Category: Saavedra MJ]]
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[[Category: Alpha-beta]]
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[[Category: Spencer J]]
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[[Category: Hydrolase]]
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[[Category: Metallo-beta-lactamase]]
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[[Category: Metalloenzyme]]
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Current revision

Crystal Structure of Serratia fonticola Sfh-I: glycerol complex

PDB ID 3q6v

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