We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1znw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1znw.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1znw.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1znw| PDB=1znw | SCENE= }}
{{STRUCTURE_1znw| PDB=1znw | SCENE= }}
-
'''Crystal Structure Of Unliganded Form Of Mycobacterium tuberculosis Guanylate Kinase'''
+
===Crystal Structure Of Unliganded Form Of Mycobacterium tuberculosis Guanylate Kinase===
-
==Overview==
+
<!--
-
Bacterial nucleoside monophosphate (NMP) kinases, which convert NMPs to nucleoside diphosphates (NDP), are investigated as potential antibacterial targets against pathogenic bacteria. Herein, we report the biochemical and structural characterization of GMP kinase from Mycobacterium tuberculosis (GMPKMt). GMPKMt is a monomer with an unusual specificity for ATP as a phosphate donor, a lower catalytic efficiency compared with eukaryotic GMPKs, and it carries two redox-sensitive cysteines in the central CORE domain. These properties were analyzed in the light of the high-resolution crystal structures of unbound, GMP-bound, and GDP-bound GMPKMt. The latter structure was obtained in both an oxidized form, in which the cysteines form a disulfide bridge, and a reduced form which is expected to correspond to the physiological enzyme. GMPKMt has a modular domain structure as most NMP kinases. However, it departs from eukaryotic GMPKs by the unusual conformation of its CORE domain, and by its partially open LID and GMP-binding domains which are the same in the apo-, GMP-bound, and GDP-bound forms. GMPKMt also features a unique GMP binding site which is less close-packed than that of mammalian GMPKs, and in which the replacement of a critical tyrosine by a serine removes a catalytic interaction. In contrast, the specificity of GMPKMt for ATP may be a general feature of GMPKs because of an invariant structural motif that recognizes the adenine base. Altogether, differences in domain dynamics and GMP binding between GMPKMt and mammalian GMPKs should reveal clues for the design of GMPKMt-specific inhibitors.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16288457}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16288457 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16288457}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Gmp kinase]]
[[Category: Gmp kinase]]
[[Category: Guanylate kinase]]
[[Category: Guanylate kinase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:51:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:58:45 2008''

Revision as of 12:58, 29 July 2008

Image:1znw.png

Template:STRUCTURE 1znw

Crystal Structure Of Unliganded Form Of Mycobacterium tuberculosis Guanylate Kinase

Template:ABSTRACT PUBMED 16288457

About this Structure

1ZNW is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Unique GMP-binding site in Mycobacterium tuberculosis guanosine monophosphate kinase., Hible G, Christova P, Renault L, Seclaman E, Thompson A, Girard E, Munier-Lehmann H, Cherfils J, Proteins. 2006 Feb 1;62(2):489-500. PMID:16288457

Page seeded by OCA on Tue Jul 29 15:58:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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