1z45: Difference between revisions

Revision as of 21:07, 28 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:1z45.png

Template:STRUCTURE 1z45

Crystal structure of the gal10 fusion protein galactose mutarotase/UDP-galactose 4-epimerase from Saccharomyces cerevisiae complexed with NAD, UDP-glucose, and galactoseCrystal structure of the gal10 fusion protein galactose mutarotase/UDP-galactose 4-epimerase from Saccharomyces cerevisiae complexed with NAD, UDP-glucose, and galactose

Template:ABSTRACT PUBMED 15795221

About this StructureAbout this Structure

1Z45 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

The molecular architecture of galactose mutarotase/UDP-galactose 4-epimerase from Saccharomyces cerevisiae., Thoden JB, Holden HM, J Biol Chem. 2005 Jun 10;280(23):21900-7. Epub 2005 Mar 28. PMID:15795221

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-[[Image:1z45.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1z45|  PDB=1z45  |  SCENE=  }}
-'''Crystal structure of the gal10 fusion protein galactose mutarotase/UDP-galactose 4-epimerase from Saccharomyces cerevisiae complexed with NAD, UDP-glucose, and galactose'''
+===Crystal structure of the gal10 fusion protein galactose mutarotase/UDP-galactose 4-epimerase from Saccharomyces cerevisiae complexed with NAD, UDP-glucose, and galactose===
-==Overview==
+<!--
-The metabolic pathway by which beta-D-galactose is converted to glucose 1-phosphate is known as the Leloir pathway and consists of four enzymes. In most organisms, these enzymes appear to exist as soluble entities in the cytoplasm. In yeast such as Saccharomyces cerevisiae, however, the first and last enzymes of the pathway, galactose mutarotase and UDP-galactose 4-epimerase, are contained within a single polypeptide chain referred to as Gal10p. Here we report the three-dimensional structure of Gal10p in complex with NAD(+), UDP-glucose, and beta-D-galactose determined to 1.85-A resolution. The enzyme is dimeric with dimensions of approximately 91 A x 135 A x 108 A and assumes an almost V-shaped appearance. The overall architecture of the individual subunits can be described in terms of two separate N- and C-terminal domains connected by a Type II turn formed by Leu-357 to Val-360. The first 356 residues of Gal10p fold into the classical bilobal topology observed for all other UDP-galactose 4-epimerases studied thus far. This N-terminal domain contains the binding sites for NAD(+) and UDP-glucose. The polypeptide chain extending from Glu-361 to Ser-699 adopts a beta-sandwich motif and harbors the binding site for beta-D-galactose. The two active sites of Gal10p are separated by over 50 A. This investigation represents the first structural analysis of a dual function enzyme in the Leloir pathway.
+The line below this paragraph, {{ABSTRACT_PUBMED_15795221}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15795221 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15795221}}
 ==About this Structure==
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 [[Category: Metabolism]]
 [[Category: Mutarotase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:09:45 2008''
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