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| - | [[Image:1t5h.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1t5h.png|left|200px]] |
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| | {{STRUCTURE_1t5h| PDB=1t5h | SCENE= }} | | {{STRUCTURE_1t5h| PDB=1t5h | SCENE= }} |
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| - | '''4-Chlorobenzoyl-CoA Ligase/Synthetase unliganded, selenomethionine'''
| + | ===4-Chlorobenzoyl-CoA Ligase/Synthetase unliganded, selenomethionine=== |
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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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15236575}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15236575 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15236575}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Lu, X.]] | | [[Category: Lu, X.]] |
| | [[Category: Adenylate-forming coenzyme a ligase domain alternation conformational change]] | | [[Category: Adenylate-forming coenzyme a ligase domain alternation conformational change]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:32:55 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:53:28 2008'' |
Revision as of 02:53, 29 July 2008
Template:STRUCTURE 1t5h
4-Chlorobenzoyl-CoA Ligase/Synthetase unliganded, selenomethionine
Template:ABSTRACT PUBMED 15236575
About this Structure
1T5H 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 Tue Jul 29 05:53:28 2008
