This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1t5h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1t5h.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1t5h.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1t5h| PDB=1t5h | SCENE= }}
{{STRUCTURE_1t5h| PDB=1t5h | SCENE= }}
-
'''4-Chlorobenzoyl-CoA Ligase/Synthetase unliganded, selenomethionine'''
+
===4-Chlorobenzoyl-CoA Ligase/Synthetase unliganded, selenomethionine===
-
==Overview==
+
<!--
-
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.
 +
-->
 +
{{ABSTRACT_PUBMED_15236575}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[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

Image:1t5h.png

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1t5h"
Personal tools