1OCX

E. coli maltose-O-acetyltransferase

1OCX の概要

• エントリーDOI: 10.2210/pdb1ocx/pdb
• 分子名称: MALTOSE O-ACETYLTRANSFERASE, TRIMETHYL LEAD ION (3 entities in total)
• 機能のキーワード: transferase, acetyl transferase, left-handed parallel beta-helix
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 61224.83

構造登録者

Lo Leggio, L.,Dal Degan, F.,Poulsen, P.,Larsen, S. (登録日: 2003-02-11, 公開日: 2003-06-12, 最終更新日: 2024-05-08)

主引用文献

Lo Leggio, L.,Degan, F.D.,Poulsen, P.,Andersen, S.M.,Larsen, S.
The Structure and Specificity of Escherichia Coli Maltose Acetyltransferase Give New Insight Into the Laca Family of Acyltransferases.
Biochemistry, 42:5225-, 2003

PubMed Abstract: 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.

PubMed: 12731863
DOI: 10.1021/BI0271446

実験手法

X-RAY DIFFRACTION (2.15 Å)