1ocx
From Proteopedia
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[[Category: left-handed parallel beta-helix]] | [[Category: left-handed parallel beta-helix]] | ||
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Revision as of 13:45, 30 October 2007
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E. COLI MALTOSE-O-ACETYLTRANSFERASE
Overview
The crystallographic three-dimensional structure of the Escherichia coli, maa gene product, previously identified as a maltose O-acetyltransferase, (MAT) [Brand, B., and Boos, W. (1991) J. Biol. Chem. 266, 14113-14118] has, been determined to 2.15 A resolution by the single anomalous dispersion, method using data from a crystal cocrystallized with trimethyllead, acetate. It is shown here that MAT acetylates glucose exclusively at the, C6 position and maltose at the C6 position of the nonreducing end glucosyl, moiety. Furthermore, MAT shows higher affinity toward artificial, substrates containing an alkyl or hydrophobic chain as well as a glucosyl, unit. The presence of a long hydrophobic patch near the acceptor site, provides the structural explanation for this preference. The, ... [(full description)]
About this Structure
1OCX is a [Single protein] structure of sequence from [Escherichia coli] with PBM as [ligand]. Active as [Maltose O-acetyltransferase], with EC number [2.3.1.79]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The structure and specificity of Escherichia coli maltose acetyltransferase give new insight into the LacA family of acyltransferases., Lo Leggio L, Dal Degan F, Poulsen P, Andersen SM, Larsen S, Biochemistry. 2003 May 13;42(18):5225-35. PMID:12731863
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