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.


1xfg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xfg.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1xfg.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xfg| PDB=1xfg | SCENE= }}
{{STRUCTURE_1xfg| PDB=1xfg | SCENE= }}
-
'''Glutaminase domain of glucosamine 6-phosphate synthase complexed with l-glu hydroxamate'''
+
===Glutaminase domain of glucosamine 6-phosphate synthase complexed with l-glu hydroxamate===
-
==Overview==
+
<!--
-
BACKGROUND: Amidotransferases use the amide nitrogen of glutamine in a number of important biosynthetic reactions. They are composed of a glutaminase domain, which catalyzes the hydrolysis of glutamine to glutamate and ammonia, and a synthetase domain, catalyzing amination of the substrate. To gain insight into the mechanism of nitrogen transfer, we examined the structure of the glutaminase domain of glucosamine 6-phosphate synthase (GLMS). RESULTS: The crystal structures of the enzyme complexed with glutamate and with a competitive inhibitor, Glu-hydroxamate, have been determined to 1.8 A resolution. The protein fold has structural homology to other members of the superfamily of N-terminal nucleophile (Ntn) hydrolases, being a sandwich of antiparallel beta sheets surrounded by two layers of alpha helices. CONCLUSIONS: The structural homology between the glutaminase domain of GLMS and that of PRPP amidotransferase (the only other Ntn amidotransferase whose structure is known) indicates that they may have diverged from a common ancestor. Cys1 is the catalytic nucleophile in GLMS, and the nucleophilic character of its thiol group appears to be increased through general base activation by its own alpha-amino group. Cys1 can adopt two conformations, one active and one inactive; glutamine binding locks the residue in a predetermined conformation. We propose that when a nitrogen acceptor is present Cys1 is kept in the active conformation, explaining the phenomenon of substrate-induced activation of the enzyme, and that Arg26 is central in this coupling.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8805567}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8805567 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8805567}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Glutamine amidotransferase]]
[[Category: Glutamine amidotransferase]]
[[Category: N-terminal nucleophile]]
[[Category: N-terminal nucleophile]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:57:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:16:11 2008''

Revision as of 03:16, 29 July 2008

Image:1xfg.png

Template:STRUCTURE 1xfg

Glutaminase domain of glucosamine 6-phosphate synthase complexed with l-glu hydroxamate

Template:ABSTRACT PUBMED 8805567

About this Structure

1XFG is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1gms. Full crystallographic information is available from OCA.

Reference

Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 A crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase., Isupov MN, Obmolova G, Butterworth S, Badet-Denisot MA, Badet B, Polikarpov I, Littlechild JA, Teplyakov A, Structure. 1996 Jul 15;4(7):801-10. PMID:8805567

Page seeded by OCA on Tue Jul 29 06:16:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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