1hxp

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(New page: 200px<br /> <applet load="1hxp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hxp, resolution 1.8&Aring;" /> '''NUCLEOTIDE TRANSFERA...)
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Revision as of 16:30, 29 October 2007


1hxp, resolution 1.8Å

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NUCLEOTIDE TRANSFERASE

Overview

Galactose-1-phosphate uridylyltransferase catalyzes the reversible, transfer of the uridine 5'-monophosphoryl moiety of UDP-glucose to the, phosphate group of galactose 1-phosphate to form UDP-galactose. This, enzyme participates in the Leloir pathway of galactose metabolism, and its, absence is the primary cause of the potentially lethal disease, galactosemia. The three-dimensional structure of the dimeric enzyme from, Escherichia coli complexed with uridine 5'-diphosphate is reported here., The structure was solved by multiple isomorphous replacement and electron, density modification techniques and has been refined to 1.8 A resolution., Enzyme subunits consist of a single domain with the topology of a, "half-barrel". The barrel staves are formed by nine strands of, antiparallel ... [(full description)]

About this Structure

1HXP is a [Single protein] structure of sequence from [Escherichia coli] with ZN, FE, BME, U5P and UDP as [ligands]. Active as [[1]], with EC number [2.7.7.10]. Full crystallographic information is available from [OCA].

Reference

Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 A resolution., Wedekind JE, Frey PA, Rayment I, Biochemistry. 1995 Sep 5;34(35):11049-61. PMID:7669762

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