1fof

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(New page: 200px<br /><applet load="1fof" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fof, resolution 2.00&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1fof.gif|left|200px]]<br /><applet load="1fof" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fof, resolution 2.00&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10==
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We report the crystal structure of a class D beta-lactamase, the broad, spectrum enzyme OXA-10 from Pseudomonas aeruginosa at 2.0 A resolution., There are significant differences between the overall fold observed in, this structure and those of the evolutionarily related class A and class C, beta-lactamases. Furthermore, the structure suggests the unique, cation, mediated formation of a homodimer. Kinetic and hydrodynamic data shows, that the dimer is a relevant species in solution and is the more active, form of the enzyme. Comparison of the molecular details of the active, sites of the class A and class C enzymes with the OXA-10 structure reveals, that there is no counterpart in OXA-10 to the residues proposed to act as, general bases in either of these enzymes (Glu 166 and Tyr 150, respectively). Our structures of the native and chloride inhibited forms, of OXA-10 suggest that the class D enzymes have evolved a distinct, catalytic mechanism for beta-lactam hydrolysis. Clinical variants of, OXA-10 are also discussed in light of the structure.
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<StructureSection load='1fof' size='340' side='right'caption='[[1fof]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fof]] 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=1FOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FOF FirstGlance]. <br>
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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]] 2&#8491;</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=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1fof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fof OCA], [https://pdbe.org/1fof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fof RCSB], [https://www.ebi.ac.uk/pdbsum/1fof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fof ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BLO10_PSEAI BLO10_PSEAI] Hydrolyzes both carbenicillin and oxacillin.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/1fof_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fof ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We report the crystal structure of a class D beta-lactamase, the broad spectrum enzyme OXA-10 from Pseudomonas aeruginosa at 2.0 A resolution. There are significant differences between the overall fold observed in this structure and those of the evolutionarily related class A and class C beta-lactamases. Furthermore, the structure suggests the unique, cation mediated formation of a homodimer. Kinetic and hydrodynamic data shows that the dimer is a relevant species in solution and is the more active form of the enzyme. Comparison of the molecular details of the active sites of the class A and class C enzymes with the OXA-10 structure reveals that there is no counterpart in OXA-10 to the residues proposed to act as general bases in either of these enzymes (Glu 166 and Tyr 150, respectively). Our structures of the native and chloride inhibited forms of OXA-10 suggest that the class D enzymes have evolved a distinct catalytic mechanism for beta-lactam hydrolysis. Clinical variants of OXA-10 are also discussed in light of the structure.
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==About this Structure==
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Crystal structure of the class D beta-lactamase OXA-10.,Paetzel M, Danel F, de Castro L, Mosimann SC, Page MG, Strynadka NC Nat Struct Biol. 2000 Oct;7(10):918-25. PMID:11017203<ref>PMID:11017203</ref>
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1FOF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with CO and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FOF OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of the class D beta-lactamase OXA-10., Paetzel M, Danel F, de Castro L, Mosimann SC, Page MG, Strynadka NC, Nat Struct Biol. 2000 Oct;7(10):918-25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11017203 11017203]
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</div>
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[[Category: Beta-lactamase]]
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<div class="pdbe-citations 1fof" style="background-color:#fffaf0;"></div>
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Single protein]]
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[[Category: Castro, L.de.]]
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[[Category: Danel, F.]]
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[[Category: Mosimann, S.C.]]
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[[Category: Paetzel, M.]]
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[[Category: Page, M.G.P.]]
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[[Category: Strynadka, N.C.J.]]
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[[Category: CO]]
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[[Category: SO4]]
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[[Category: beta-lactamase]]
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[[Category: class-d]]
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[[Category: cobalt]]
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[[Category: oxa-10]]
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[[Category: oxacillinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:05:32 2007''
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==See Also==
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Danel F]]
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[[Category: Mosimann SC]]
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[[Category: Paetzel M]]
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[[Category: Page MGP]]
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[[Category: Strynadka NCJ]]
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[[Category: De Castro L]]

Current revision

CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10

PDB ID 1fof

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