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.


2p2b

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2p2b.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2p2b.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2p2b| PDB=2p2b | SCENE= }}
{{STRUCTURE_2p2b| PDB=2p2b | SCENE= }}
-
'''Acetyl-CoA Synthetase, V386A mutation'''
+
===Acetyl-CoA Synthetase, V386A mutation===
-
==Overview==
+
<!--
-
The adenylate-forming enzymes, including acyl-CoA synthetases, the adenylation domains of non-ribosomal peptide synthetases (NRPS), and firefly luciferase, perform two half-reactions in a ping-pong mechanism. We have proposed a domain alternation mechanism for these enzymes whereby, upon completion of the initial adenylation reaction, the C-terminal domain of these enzymes undergoes a 140 degrees rotation to perform the second thioester-forming half-reaction. Structural and kinetic data of mutant enzymes support this hypothesis. We present here mutations to Salmonella enterica acetyl-CoA synthetase (Acs) and test the ability of the enzymes to catalyze the complete reaction and the adenylation half-reaction. Substitution of Lys609 with alanine results in an enzyme that is unable to catalyze the adenylate reaction, while the Gly524 to leucine substitution is unable to catalyze the complete reaction yet catalyzes the adenylation half-reaction with activity comparable to the wild-type enzyme. The positions of these two residues, which are located on the mobile C-terminal domain, strongly support the domain alternation hypothesis. We also present steady-state kinetic data of putative substrate-binding residues and demonstrate that no single residue plays a dominant role in dictating CoA binding. We have also created two mutations in the active site to alter the acyl substrate specificity. Finally, the crystallographic structures of wild-type Acs and mutants R194A, R584A, R584E, K609A, and V386A are presented to support the biochemical analysis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17497934}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17497934 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17497934}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Adenylate-forming enzyme]]
[[Category: Adenylate-forming enzyme]]
[[Category: Domain alternation]]
[[Category: Domain alternation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:11:24 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:24:42 2008''

Revision as of 01:24, 28 July 2008

Image:2p2b.png

Template:STRUCTURE 2p2b

Acetyl-CoA Synthetase, V386A mutation

Template:ABSTRACT PUBMED 17497934

About this Structure

2P2B is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

Biochemical and crystallographic analysis of substrate binding and conformational changes in acetyl-CoA synthetase., Reger AS, Carney JM, Gulick AM, Biochemistry. 2007 Jun 5;46(22):6536-46. Epub 2007 May 12. PMID:17497934

Page seeded by OCA on Mon Jul 28 04:24:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2p2b"
Personal tools