1fof
From Proteopedia
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- | [[Image:1fof.gif|left|200px]] | + | [[Image:1fof.gif|left|200px]] |
- | + | ||
- | '''CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10''' | + | {{Structure |
+ | |PDB= 1fof |SIZE=350|CAPTION= <scene name='initialview01'>1fof</scene>, resolution 2.00Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
+ | |ACTIVITY= [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] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1FOF is a [ | + | 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]. |
==Reference== | ==Reference== | ||
- | 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:// | + | 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] |
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
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[[Category: oxacillinase]] | [[Category: oxacillinase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:11:49 2008'' |
Revision as of 09:11, 20 March 2008
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, resolution 2.00Å | |||||||
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Ligands: | and | ||||||
Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10
Overview
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
1FOF is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 11:11:49 2008
Categories: Beta-lactamase | Pseudomonas aeruginosa | Single protein | Castro, L de. | Danel, F. | Mosimann, S C. | Paetzel, M. | Page, M G.P. | Strynadka, N C.J. | CO | SO4 | Class-d | Cobalt | Oxa-10 | Oxacillinase