1ocx

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(New page: 200px<br /> <applet load="1ocx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ocx, resolution 2.15&Aring;" /> '''E. COLI MALTOSE-O-A...)
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==About this Structure==
==About this Structure==
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1OCX is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with PBM as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.79 2.3.1.79]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OCX OCA]].
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1OCX is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with PBM as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Maltose_O-acetyltransferase Maltose O-acetyltransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.79 2.3.1.79]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OCX OCA]].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12731863 12731863]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12731863 12731863]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Maltose O-acetyltransferase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Degan, F.D.]]
[[Category: Degan, F.D.]]
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[[Category: left-handed parallel beta-helix]]
[[Category: left-handed parallel beta-helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 22:11:01 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:33:42 2007''

Revision as of 12:28, 30 October 2007


1ocx, resolution 2.15Å

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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

Page seeded by OCA on Tue Oct 30 14:33:42 2007

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