1fof
From Proteopedia
(New page: 200px<br /><applet load="1fof" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fof, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1fof.gif|left|200px]]<br /><applet load="1fof" size=" | + | [[Image:1fof.gif|left|200px]]<br /><applet load="1fof" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fof, resolution 2.00Å" /> | caption="1fof, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10'''<br /> | '''CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We report the crystal structure of a class D beta-lactamase, the broad | + | 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== | ==About this Structure== | ||
| - | 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:// | + | 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 <scene name='pdbligand=CO:'>CO</scene> and <scene name='pdbligand=SO4:'>SO4</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Castro, L | + | [[Category: Castro, L de.]] |
[[Category: Danel, F.]] | [[Category: Danel, F.]] | ||
| - | [[Category: Mosimann, S | + | [[Category: Mosimann, S C.]] |
[[Category: Paetzel, M.]] | [[Category: Paetzel, M.]] | ||
| - | [[Category: Page, M | + | [[Category: Page, M G.P.]] |
| - | [[Category: Strynadka, N | + | [[Category: Strynadka, N C.J.]] |
[[Category: CO]] | [[Category: CO]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
| Line 28: | Line 28: | ||
[[Category: oxacillinase]] | [[Category: oxacillinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:55 2008'' |
Revision as of 10:40, 21 February 2008
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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 with and as ligands. Active as Beta-lactamase, with EC number 3.5.2.6 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 Feb 21 12:40:55 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
