|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of the closed form of Pseudomonas aeruginosa SPM-1== | | ==Crystal structure of the closed form of Pseudomonas aeruginosa SPM-1== |
| - | <StructureSection load='4bp0' size='340' side='right' caption='[[4bp0]], [[Resolution|resolution]] 2.24Å' scene=''> | + | <StructureSection load='4bp0' size='340' side='right'caption='[[4bp0]], [[Resolution|resolution]] 2.24Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4bp0]] is a 4 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=4BP0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BP0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4bp0]] is a 4 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=4BP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BP0 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=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]] 2.24Å</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='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=ZN:ZINC+ION'>ZN</scene></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=4bp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bp0 OCA], [http://pdbe.org/4bp0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bp0 RCSB], [http://www.ebi.ac.uk/pdbsum/4bp0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bp0 ProSAT]</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=4bp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bp0 OCA], [https://pdbe.org/4bp0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bp0 RCSB], [https://www.ebi.ac.uk/pdbsum/4bp0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bp0 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 == |
| Line 19: |
Line 21: |
| | | | |
| | ==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: Brem, J]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: McDonough, M A]] | + | [[Category: Brem J]] |
| - | [[Category: Schofield, C J]]
| + | [[Category: McDonough MA]] |
| - | [[Category: Hydrolase]] | + | [[Category: Schofield CJ]] |
| - | [[Category: Metallo beta lactamase]] | + | |
| Structural highlights
Function
Q8G9Q0_PSEAI
Publication Abstract from PubMed
Metallo-beta-lactamases (MBLs) catalyse the hydrolysis of almost all beta-lactam antibiotics. We report biophysical and kinetic studies on the Sao Paulo MBL (SPM-1), which reveal its Zn(ii) ion usage and mechanism as characteristic of the clinically important di-Zn(ii) dependent B1 MBL subfamily. Biophysical analyses employing crystallography, dynamic 19F NMR and ion mobility mass spectrometry, however, reveal that SPM-1 possesses loop and mobile element regions characteristic of the B2 MBLs. These include a mobile alpha3 region which is important in catalysis and determining inhibitor selectivity. SPM-1 thus appears to be a hybrid B1/B2 MBL. The results have implications for MBL evolution and inhibitor design.
Studying the active-site loop movement of the Sao Paolo metallo-beta-lactamase-1daggerElectronic supplementary information (ESI) available: Procedures for protein expression and purification, F-labelling, crystallisation, data collection, and structure determination, table of crystallographic data, table of crystallographic parameters and refinement statistics, figures showing binding mode and distances, procedures for mass spectrometry measurements, differential scanning fluorimetry measurements, stopped-flow measurements and other kinetics measurements. See DOI: 10.1039/c4sc01752hClick here for additional data file.,Brem J, Struwe WB, Rydzik AM, Tarhonskaya H, Pfeffer I, Flashman E, van Berkel SS, Spencer J, Claridge TD, McDonough MA, Benesch JL, Schofield CJ Chem Sci. 2015 Feb 19;6(2):956-963. Epub 2014 Nov 4. PMID:25717359[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Brem J, Struwe WB, Rydzik AM, Tarhonskaya H, Pfeffer I, Flashman E, van Berkel SS, Spencer J, Claridge TD, McDonough MA, Benesch JL, Schofield CJ. Studying the active-site loop movement of the Sao Paolo metallo-beta-lactamase-1daggerElectronic supplementary information (ESI) available: Procedures for protein expression and purification, F-labelling, crystallisation, data collection, and structure determination, table of crystallographic data, table of crystallographic parameters and refinement statistics, figures showing binding mode and distances, procedures for mass spectrometry measurements, differential scanning fluorimetry measurements, stopped-flow measurements and other kinetics measurements. See DOI: 10.1039/c4sc01752hClick here for additional data file. Chem Sci. 2015 Feb 19;6(2):956-963. Epub 2014 Nov 4. PMID:25717359 doi:http://dx.doi.org/10.1039/c4sc01752h
|
