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[[Image:1fof.gif|left|200px]]
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{{STRUCTURE_1fof|  PDB=1fof  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10'''


==CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10==
<StructureSection load='1fof' size='340' side='right'caption='[[1fof]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BLO10_PSEAI BLO10_PSEAI] Hydrolyzes both carbenicillin and oxacillin.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/1fof_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1FOF is a [[Single protein]] structure of sequence from [http://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].
</div>
<div class="pdbe-citations 1fof" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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://www.ncbi.nlm.nih.gov/pubmed/11017203 11017203]
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
[[Category: Beta-lactamase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Danel F]]
[[Category: Castro, L de.]]
[[Category: Mosimann SC]]
[[Category: Danel, F.]]
[[Category: Paetzel M]]
[[Category: Mosimann, S C.]]
[[Category: Page MGP]]
[[Category: Paetzel, M.]]
[[Category: Strynadka NCJ]]
[[Category: Page, M G.P.]]
[[Category: De Castro L]]
[[Category: Strynadka, N C.J.]]
[[Category: Beta-lactamase]]
[[Category: Class-d]]
[[Category: Cobalt]]
[[Category: Oxa-10]]
[[Category: Oxacillinase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:34:26 2008''