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.

2va1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2va1.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2va1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2va1| PDB=2va1 | SCENE= }}
{{STRUCTURE_2va1| PDB=2va1 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF UMP KINASE FROM UREAPLASMA PARVUM'''
+
===CRYSTAL STRUCTURE OF UMP KINASE FROM UREAPLASMA PARVUM===
-
==Overview==
+
<!--
-
The crystal structure of uridine monophosphate kinase (UMP kinase, UMPK) from the opportunistic pathogen Ureaplasma parvum was determined and showed similar three-dimensional fold as other bacterial and archaeal UMPKs that all belong to the amino acid kinase family. Recombinant UpUMPK exhibited Michaelis-Menten kinetics with UMP, with K(m) and V(max) values of 214 +/- 4 microm and 262 +/- 24 micromol.min(-1).mg(-1), respectively, but with ATP as variable substrate the kinetic analysis showed positive cooperativity, with an n value of 1.5 +/- 0.1. The end-product UTP was a competitive inhibitor against UMP and a noncompetitive inhibitor towards ATP. Unlike UMPKs from other bacteria, which are activated by GTP, GTP had no detectable effect on UpUMPK activity. An attempt to create a GTP-activated enzyme was made using site-directed mutagenesis. The mutant enzyme F133N (F133 corresponds to the residue in Escherichia coli that is involved in GTP activation), with F133A as a control, were expressed, purified and characterized. Both enzymes exhibited negative cooperativity with UMP, and GTP had no effect on enzyme activity, demonstrating that F133 is involved in subunit interactions but apparently not in GTP activation. The physiological role of UpUMPK in bacterial nucleic acid synthesis and its potential as target for development of antimicrobial agents are discussed.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18021254}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18021254 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18021254}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Umpk]]
[[Category: Umpk]]
[[Category: Uridylate kinase]]
[[Category: Uridylate kinase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:28:05 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:57:31 2008''

Revision as of 15:57, 28 July 2008

Image:2va1.png

Template:STRUCTURE 2va1

CRYSTAL STRUCTURE OF UMP KINASE FROM UREAPLASMA PARVUM

Template:ABSTRACT PUBMED 18021254

About this Structure

2VA1 is a Single protein structure of sequence from Ureaplasma parvum. Full crystallographic information is available from OCA.

Reference

Structural and functional investigations of Ureaplasma parvum UMP kinase--a potential antibacterial drug target., Egeblad-Welin L, Welin M, Wang L, Eriksson S, FEBS J. 2007 Dec;274(24):6403-14. Epub 2007 Nov 15. PMID:18021254

Page seeded by OCA on Mon Jul 28 18:57:31 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2va1"
Personal tools