2pa4: Difference between revisions

Revision as of 02:37, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2pa4.png

Template:STRUCTURE 2pa4

Crystal structure of UDP-glucose pyrophosphorylase from Corynebacteria glutamicum in complex with magnesium and UDP-glucoseCrystal structure of UDP-glucose pyrophosphorylase from Corynebacteria glutamicum in complex with magnesium and UDP-glucose

Template:ABSTRACT PUBMED 17567737

About this StructureAbout this Structure

2PA4 is a Single protein structure of sequence from Corynebacterium glutamicum. Full crystallographic information is available from OCA.

ReferenceReference

Active site geometry of glucose-1-phosphate uridylyltransferase., Thoden JB, Holden HM, Protein Sci. 2007 Jul;16(7):1379-88. Epub 2007 Jun 13. PMID:17567737

Page seeded by OCA on Tue Jul 29 02:37:04 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2pa4.gif|left|200px]]
+{{Seed}}
+[[Image:2pa4.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2pa4|  PDB=2pa4  |  SCENE=  }}
-'''Crystal structure of UDP-glucose pyrophosphorylase from Corynebacteria glutamicum in complex with magnesium and UDP-glucose'''
+===Crystal structure of UDP-glucose pyrophosphorylase from Corynebacteria glutamicum in complex with magnesium and UDP-glucose===
-==Overview==
+<!--
-Glucose-1-phosphate uridylyltransferase, or UGPase, catalyzes the production of UDP-glucose from glucose-1-phosphate and UTP. Because of the biological role of UDP-glucose in glycogen synthesis and in the formation of glycolipids, glycoproteins, and proteoglycans, the enzyme is widespread in nature. Recently this laboratory reported the three-dimensional structure of UGPase from Escherichia coli. While the initial X-ray analysis revealed the overall fold of the enzyme, details concerning its active site geometry were limited because crystals of the protein complexed with either substrates or products could never be obtained. In an effort to more fully investigate the active site geometry of the enzyme, UGPase from Corynebacterium glutamicum was subsequently cloned and purified. Here we report the X-ray structure of UGPase crystallized in the presence of both magnesium and UDP-glucose. Residues involved in anchoring the ligand to the active site include the polypeptide chain backbone atoms of Ala 20, Gly 21, Gly 117, Gly 180, and Ala 214, and the side chains of Glu 36, Gln 112, Asp 143, Glu 201, and Lys 202. Two magnesium ions are observed coordinated to the UDP-glucose. An alpha- and a beta-phosphoryl oxygen, three waters, and the side chain of Asp 142 ligate the first magnesium, whereas the second ion is coordinated by an alpha-phosphoryl oxygen and five waters. The position of the first magnesium is conserved in both the glucose-1-phosphate thymidylyltransferases and the cytidylyltransferases. The structure presented here provides further support for the role of the conserved magnesium ion in the catalytic mechanisms of the sugar-1-phosphate nucleotidylyltransferases.
+The line below this paragraph, {{ABSTRACT_PUBMED_17567737}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17567737 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17567737}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Nucleotidyltransferase]]
 [[Category: Phosphorylase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 12:42:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:37:04 2008''