1l7k: Difference between revisions

Revision as of 11:53, 2 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:1l7k.png

Template:STRUCTURE 1l7k

x-ray structure of galactose mutarotase from Lactococcus lactis complexed with galactosex-ray structure of galactose mutarotase from Lactococcus lactis complexed with galactose

Template:ABSTRACT PUBMED 11907040

About this StructureAbout this Structure

1L7K is a Single protein structure of sequence from Lactococcus lactis. Full crystallographic information is available from OCA.

ReferenceReference

High resolution X-ray structure of galactose mutarotase from Lactococcus lactis., Thoden JB, Holden HM, J Biol Chem. 2002 Jun 7;277(23):20854-61. Epub 2002 Mar 20. PMID:11907040

Page seeded by OCA on Wed Jul 2 11:52:52 2008

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-[[Image:1l7k.gif|left|200px]]
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 {{STRUCTURE_1l7k|  PDB=1l7k  |  SCENE=  }}
-'''x-ray structure of galactose mutarotase from Lactococcus lactis complexed with galactose'''
+===x-ray structure of galactose mutarotase from Lactococcus lactis complexed with galactose===
-==Overview==
+<!--
-Galactose mutarotase plays a key role in normal galactose metabolism by catalyzing the interconversion of beta-D-galactose and alpha-D-galactose. Here we describe the three-dimensional architecture of galactose mutarotase from Lactococcus lactis determined to 1.9-A resolution. Each subunit of the dimeric enzyme displays a distinctive beta-sandwich motif. This tertiary structural element was first identified in beta-galactosidase and subsequently observed in copper amine oxidase, hyaluronate lyase, chondroitinase, and maltose phosphorylase. Two cis-peptides are found in each subunit, namely Pro(67) and Lys(136). The active site is positioned in a rather open cleft, and the electron density corresponding to the bound galactose unequivocally demonstrates that both anomers of the substrate are present in the crystalline enzyme. Those residues responsible for anchoring the sugar to the protein include Arg(71), His(96), His(170), Asp(243), and Glu(304). Both His(96) and His(170) are strictly conserved among mutarotase amino acid sequences determined thus far. The imidazole nitrogens of these residues are located within hydrogen bonding distance to the C-5 oxygen of galactose. Strikingly, the carboxylate group of Glu(304) is situated at approximately 2.7 A from the 1'-hydroxyl group of galactose, thereby suggesting its possible role as a general acid/base group.
+The line below this paragraph, {{ABSTRACT_PUBMED_11907040}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11907040 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11907040}}
 ==About this Structure==
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 [[Category: Galactose metabolism]]
 [[Category: Mutarotase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:37:58 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 11:52:52 2008''