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.


2bne

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2bne.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2bne.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2bne| PDB=2bne | SCENE= }}
{{STRUCTURE_2bne| PDB=2bne | SCENE= }}
-
'''THE STRUCTURE OF E. COLI UMP KINASE IN COMPLEX WITH UMP'''
+
===THE STRUCTURE OF E. COLI UMP KINASE IN COMPLEX WITH UMP===
-
==Overview==
+
<!--
-
Bacterial UMP kinases are essential enzymes involved in the multistep synthesis of nucleoside triphosphates. They are hexamers regulated by the allosteric activator GTP and inhibited by UTP. We solved the crystal structure of Escherichia coli UMP kinase bound to the UMP substrate (2.3 A resolution), the UDP product (2.6 A), or UTP (2.45 A). The monomer fold, unrelated to that of other nucleoside monophosphate kinases, belongs to the carbamate kinase-like superfamily. However, the phosphate acceptor binding cleft and subunit assembly are characteristic of UMP kinase. Interactions with UMP explain the high specificity for this natural substrate. UTP, previously described as an allosteric inhibitor, was unexpectedly found in the phosphate acceptor site, suggesting that it acts as a competitive inhibitor. Site-directed mutagenesis of residues Thr-138 and Asn-140, involved in both uracil recognition and active site interaction within the hexamer, decreased the activation by GTP and inhibition by UTP. These experiments suggest a cross-talk mechanism between enzyme subunits involved in cooperative binding at the phosphate acceptor site and in allosteric regulation by GTP. As bacterial UMP kinases have no counterpart in eukaryotes, the information provided here could help the design of new antibiotics.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15857829}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15857829 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15857829}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Pyrimidine biosynthesis]]
[[Category: Pyrimidine biosynthesis]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:31:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:57:41 2008''

Revision as of 18:57, 27 July 2008

Image:2bne.png

Template:STRUCTURE 2bne

THE STRUCTURE OF E. COLI UMP KINASE IN COMPLEX WITH UMP

Template:ABSTRACT PUBMED 15857829

About this Structure

2BNE is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of Escherichia coli UMP kinase differs from that of other nucleoside monophosphate kinases and sheds new light on enzyme regulation., Briozzo P, Evrin C, Meyer P, Assairi L, Joly N, Barzu O, Gilles AM, J Biol Chem. 2005 Jul 8;280(27):25533-40. Epub 2005 Apr 27. PMID:15857829

Page seeded by OCA on Sun Jul 27 21:57:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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