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.

2i5k

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2i5k.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2i5k.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2i5k| PDB=2i5k | SCENE= }}
{{STRUCTURE_2i5k| PDB=2i5k | SCENE= }}
-
'''Crystal structure of Ugp1p'''
+
===Crystal structure of Ugp1p===
-
==Overview==
+
<!--
-
UDP-glucose is the universal activated form of glucose, employed in all organisms for glucosyl transfer reactions and as precursor for various activated carbohydrates. In animal and fungal metabolism, UDP-glucose is required for utilization of galactose and for the synthesis of glycogen, the major carbohydrate storage polymer. The formation of UDP-glucose is catalyzed by UDP-glucose pyrophosphorylase (UGPase), which is highly conserved among eukaryotes. Here, we present the crystal structure of yeast UGPase, Ugp1p. Both in solution and in the crystal, Ugp1p forms homooctamers, which represent the enzymatically active form of the protein. Ugp1p subunits consist of three domains, with the active site presumably located in the central SpsA GnT I core (SGC) domain. The association in the octamer is mediated by contacts between left-handed beta-helices in the C-terminal domains, forming a toroidal solenoid structure in the core of the complex. The catalytic domains attached to this scaffold core do not directly contact each other, consistent with simple Michaelis-Menten kinetics found for Ugp1p. Conservation of hydrophobic residues at the subunit interfaces suggests that all fungal and animal homologs form this quarternary structure arrangement in contrast to monomeric plant UGPases, which have charged residues at these positions. Implications of this oligomeric arrangement for regulation of UGPase activity in fungi and animals are discussed.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17010990}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17010990 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17010990}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Left-handed beta-helix]]
[[Category: Left-handed beta-helix]]
[[Category: Sgc domain]]
[[Category: Sgc domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:05:59 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:27:35 2008''

Revision as of 16:27, 27 July 2008

Image:2i5k.png

Template:STRUCTURE 2i5k

Crystal structure of Ugp1p

Template:ABSTRACT PUBMED 17010990

About this Structure

2I5K is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structural basis for subunit assembly in UDP-glucose pyrophosphorylase from Saccharomyces cerevisiae., Roeben A, Plitzko JM, Korner R, Bottcher UM, Siegers K, Hayer-Hartl M, Bracher A, J Mol Biol. 2006 Dec 8;364(4):551-60. Epub 2006 Sep 1. PMID:17010990

Page seeded by OCA on Sun Jul 27 19:27:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2i5k"
Personal tools