2j5s
From Proteopedia
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| - | [[Image:2j5s. | + | [[Image:2j5s.jpg|left|200px]]<br /><applet load="2j5s" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2j5s" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2j5s, resolution 1.57Å" /> | caption="2j5s, resolution 1.57Å" /> | ||
'''STRUCTURAL OF ABDH, A BETA-DIKETONE HYDROLASE FROM THE CYANOBACTERIUM ANABAENA SP. PCC 7120 BOUND TO (S)-3-OXOCYCLOHEXYL ACETIC ACID'''<br /> | '''STRUCTURAL OF ABDH, A BETA-DIKETONE HYDROLASE FROM THE CYANOBACTERIUM ANABAENA SP. PCC 7120 BOUND TO (S)-3-OXOCYCLOHEXYL ACETIC ACID'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2J5S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with NI and KTA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-diketone_hydrolase Beta-diketone hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.7.1.7 3.7.1.7] | + | 2J5S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with NI and KTA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-diketone_hydrolase Beta-diketone hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.7.1.7 3.7.1.7] Known structural/functional Site: <scene name='pdbsite=AC1:Ni Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J5S OCA]. |
==Reference== | ==Reference== | ||
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[[Category: lyase]] | [[Category: lyase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:50:00 2007'' |
Revision as of 17:40, 18 December 2007
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STRUCTURAL OF ABDH, A BETA-DIKETONE HYDROLASE FROM THE CYANOBACTERIUM ANABAENA SP. PCC 7120 BOUND TO (S)-3-OXOCYCLOHEXYL ACETIC ACID
Overview
The gene alr4455 from the well-studied cyanobacterium Anabaena sp. PCC, 7120 encodes a crotonase orthologue that displays beta-diketone hydrolase, activity. Anabaena beta-diketone hydrolase (ABDH), in common with, 6-oxocamphor hydrolase (OCH) from Rhodococcus sp. NCIMB 9784, catalyzes, the desymmetrization of bicyclo[2.2.2]octane-2,6-dione to yield, [(S)-3-oxocyclohexyl]acetic acid, a reaction unusual among the crotonase, superfamily as the substrate is not an acyl-CoA thioester. The structure, of ABDH has been determined to a resolution of 1.5 A in both native and, ligand-bound forms. ABDH forms a hexamer similar to OCH and features one, active site per enzyme monomer. The arrangement of side chains in the, active site indicates that while the catalytic chemistry may be conserved, in OCH orthologues, the structural determinants of substrate specificity, are different. In the active site of ligand-bound forms that had been, cocrystallized with the bicyclic diketone substrate, bicyclo[2.2.2]octane-2,6-dione was found the product of the asymmetric, enzymatic retro-Claisen reaction [(S)-3-oxocyclohexyl]acetic acid. The, structures of ABDH in both native and ligand-bound forms reveal further, details about structural variation and modes of coenzyme A-independent, activity within the crotonases and provide further evidence of a wider, suprafamily of enzymes that have recruited the crotonase fold for the, catalysis of reactions other than those regularly attributed to canonical, superfamily members.
About this Structure
2J5S is a Single protein structure of sequence from Anabaena sp. with NI and KTA as ligands. Active as Beta-diketone hydrolase, with EC number 3.7.1.7 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structural characterization of a beta-diketone hydrolase from the cyanobacterium Anabaena sp. PCC 7120 in native and product-bound forms, a coenzyme A-independent member of the crotonase suprafamily., Bennett JP, Whittingham JL, Brzozowski AM, Leonard PM, Grogan G, Biochemistry. 2007 Jan 9;46(1):137-44. PMID:17198383
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