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==Crystal structure of metallo-beta-lactamase SPM-1 in space group P4222==
==Crystal structure of metallo-beta-lactamase SPM-1 in space group P4222==
<StructureSection load='5nde' size='340' side='right' caption='[[5nde]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='5nde' size='340' side='right'caption='[[5nde]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5nde]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NDE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NDE FirstGlance]. <br>
<table><tr><td colspan='2'>[[5nde]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NDE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.7&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spm-1, bla SPM-1, blaSPM-1, CCBH4851_00081, ICEPaeSP_00028 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5nde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nde OCA], [https://pdbe.org/5nde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nde RCSB], [https://www.ebi.ac.uk/pdbsum/5nde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nde ProSAT]</span></td></tr>
<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=5nde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nde OCA], [http://pdbe.org/5nde PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nde RCSB], [http://www.ebi.ac.uk/pdbsum/5nde PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nde ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8G9Q0_PSEAI Q8G9Q0_PSEAI]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Beta-lactamase|Beta-lactamase]]
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Beta-lactamase]]
[[Category: Large Structures]]
[[Category: Hinchliffe, P]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Spencer, J]]
[[Category: Hinchliffe P]]
[[Category: Cyclobutanone]]
[[Category: Spencer J]]
[[Category: Hydrolase]]
[[Category: Inhibitor]]
[[Category: Lactamase]]

Latest revision as of 15:48, 15 November 2023

Crystal structure of metallo-beta-lactamase SPM-1 in space group P4222Crystal structure of metallo-beta-lactamase SPM-1 in space group P4222

Structural highlights

5nde is a 2 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8G9Q0_PSEAI

Publication Abstract from PubMed

The most important resistance mechanism to beta-lactam antibiotics involves hydrolysis by two beta-lactamase categories: the nucleophilic serine (SBL) and the metallo- (MBL) beta-lactamases. Cyclobutanones are hydrolytically stable beta-lactam analogues with potential to inhibit both SBLs and MBLs. We describe solution and crystallographic studies on the interaction of a cyclobutanone penem analogue with the clinically important MBL SPM-1. NMR experiments using 19F-labeled SPM-1 imply the cyclobutanone binds to SPM-1 with micromolar affinity. A crystal structure of the SPM-1:cyclobutanone complex reveals binding of the hydrated cyclobutanone via interactions with one of the zinc ions, stabilisation of the hydrate by hydrogen bonding to zinc-bound water, and hydrophobic contacts with aromatic residues. NMR analyses using a 13C-labeled cyclobutanone support assignment of the bound species as the hydrated ketone. The results inform on how MBLs bind substrates and stabilize tetrahedral intermediates. They support further investigations on the use of transition state and/or intermediate analogues as inhibitors of all beta-lactamase classes.

Cyclobutanone Mimics of Intermediates in Metallo-beta-Lactamase Catalysis.,Abboud MI, Kosmopoulou M, Krismanich A, Johnson JW, Hinchliffe P, Brem J, Claridge TDW, Spencer J, Schofield C, Dmitrienko GI Chemistry. 2017 Dec 17. doi: 10.1002/chem.201705886. PMID:29250863[1]

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

See Also

References

  1. ↑ Abboud MI, Kosmopoulou M, Krismanich A, Johnson JW, Hinchliffe P, Brem J, Claridge TDW, Spencer J, Schofield C, Dmitrienko GI. Cyclobutanone Mimics of Intermediates in Metallo-beta-Lactamase Catalysis. Chemistry. 2017 Dec 17. doi: 10.1002/chem.201705886. PMID:29250863 doi:http://dx.doi.org/10.1002/chem.201705886

5nde, resolution 1.70Å

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