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| - | [[Image:1ocx.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ocx| PDB=1ocx | SCENE= }} | | {{STRUCTURE_1ocx| PDB=1ocx | SCENE= }} |
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| - | '''E. COLI MALTOSE-O-ACETYLTRANSFERASE'''
| + | ===E. COLI MALTOSE-O-ACETYLTRANSFERASE=== |
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| - | ==Overview==
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| - | 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 three-dimensional structure reveals the expected trimeric left-handed parallel beta-helix structure found in all other known hexapeptide repeat enzymes. In particular, the structure shows similarities both overall and at the putative active site to the recently determined structure of galactoside acetyltransferase (GAT), the lacA gene product [Wang, X.-G., Olsen, L. R., and Roderick, S. L. (2002) Structure 10, 581-588]. The structure, together with the new biochemical data, suggests that GAT and MAT are more closely related than previously thought and might have similar cellular functions. However, while GAT is specific for acetylation of galactosyl units, MAT is specific for glucosyl units and is able to acetylate maltooligosaccharides, an important property for biotechnological applications. Structural differences at the acceptor site reflect the differences in substrate specificity.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12731863}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12731863 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12731863}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Acetyl transferase]] | | [[Category: Acetyl transferase]] |
| | [[Category: Left-handed parallel beta-helix]] | | [[Category: Left-handed parallel beta-helix]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:40:51 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:46:37 2008'' |
Revision as of 16:46, 27 July 2008
Template:STRUCTURE 1ocx
E. COLI MALTOSE-O-ACETYLTRANSFERASE
Template:ABSTRACT PUBMED 12731863
About this Structure
1OCX is a Single protein structure of sequence from Escherichia coli. 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 Sun Jul 27 19:46:37 2008
