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1t5d

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[[Image:1t5d.gif|left|200px]]
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{{STRUCTURE_1t5d| PDB=1t5d | SCENE= }}
{{STRUCTURE_1t5d| PDB=1t5d | SCENE= }}
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'''4-Chlorobenzoyl-CoA Ligase/Synthetase bound to 4-chlorobenzoate'''
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===4-Chlorobenzoyl-CoA Ligase/Synthetase bound to 4-chlorobenzoate===
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==Overview==
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4-Chlorobenzoate:CoA ligase (CBAL) is a member of a family of adenylate-forming enzymes that catalyze two-step adenylation and thioester-forming reactions. In previous studies, we have provided structural evidence that members of this enzyme family (exemplified by acetyl-CoA synthetase) use a large domain rotation to catalyze the respective partial reactions [A. M. Gulick, V. J. Starai, A. R. Horswill, K. M. Homick, and J. C. Escalante-Semerena, (2003) Biochemistry 42, 2866-2873]. CBAL catalyzes the synthesis of 4-chlorobenzoyl-CoA, the first step in the 4-chlorobenzoate degredation pathway in PCB-degrading bacteria. We have solved the 2.0 A crystal structure of the CBAL enzyme from Alcaligenes sp. AL3007 using multiwavelength anomalous dispersion. The results demonstrate that in the absence of any ligands, or bound to the aryl substrate 4-chlorobenzoate, the enzyme adopts the conformation poised for catalysis of the adenylate-forming half-reaction. We hypothesize that coenzyme A binding is required for stabilization of the alternate conformation, which catalyzes the 4-CBA-CoA thioester-forming reaction. We have also determined the structure of the enzyme bound to the aryl substrate 4-chlorobenzoate. The aryl binding pocket is composed of Phe184, His207, Val208, Val209, Phe249, Ala280, Ile303, Gly305, Met310, and Asn311. The structure of the 4-chlorobenzoate binding site is discussed in the context of the binding sites of other family members to gain insight into substrate specificity and evolution of new function.
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{{ABSTRACT_PUBMED_15236575}}
==About this Structure==
==About this Structure==
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[[Category: Domain alternation]]
[[Category: Domain alternation]]
[[Category: Ligase]]
[[Category: Ligase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:25:53 2008''

Revision as of 03:25, 28 July 2008

Image:1t5d.png

Template:STRUCTURE 1t5d

4-Chlorobenzoyl-CoA Ligase/Synthetase bound to 4-chlorobenzoate

Template:ABSTRACT PUBMED 15236575

About this Structure

1T5D is a Single protein structure of sequence from Alcaligenes sp. al3007. Full crystallographic information is available from OCA.

Reference

Crystal structure of 4-chlorobenzoate:CoA ligase/synthetase in the unliganded and aryl substrate-bound states., Gulick AM, Lu X, Dunaway-Mariano D, Biochemistry. 2004 Jul 13;43(27):8670-9. PMID:15236575

Page seeded by OCA on Mon Jul 28 06:25:53 2008

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