1gjw

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1gjw, resolution 2.1Å

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THERMOTOGA MARITIMA MALTOSYLTRANSFERASE COMPLEX WITH MALTOSE

Overview

Maltosyltransferase (MTase) from the hyperthermophile Thermotoga maritima, represents a novel maltodextrin glycosyltransferase acting on starch and, malto-oligosaccharides. It catalyzes the transfer of maltosyl units from, alpha-1,4-linked glucans or malto-oligosaccharides to other, alpha-1,4-linked glucans, malto-oligosaccharides or glucose. It belongs to, the glycoside hydrolase family 13, which represents a large group of, (beta/alpha)(8) barrel proteins sharing a similar active site structure., The crystal structures of MTase and its complex with maltose have been, determined at 2.4 A and 2.1 A resolution, respectively. MTase is a, homodimer, each subunit of which consists of four domains, two of which, are structurally homologous to those of other family 13 enzymes. The, catalytic ... [(full description)]

About this Structure

1GJW is a [Single protein] structure of sequence from [Thermotoga maritima] with MAL, GLC and PO4 as [ligands]. Structure known Active Sites: GLC and MAL. Full crystallographic information is available from [OCA].

Reference

The crystal structure of Thermotoga maritima maltosyltransferase and its implications for the molecular basis of the novel transfer specificity., Roujeinikova A, Raasch C, Burke J, Baker PJ, Liebl W, Rice DW, J Mol Biol. 2001 Sep 7;312(1):119-31. PMID:11545590

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