1eu8

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(New page: 200px<br /><applet load="1eu8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eu8, resolution 1.9&Aring;" /> '''STRUCTURE OF TREHALOS...)
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Revision as of 20:42, 24 November 2007


1eu8, resolution 1.9Å

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STRUCTURE OF TREHALOSE MALTOSE BINDING PROTEIN FROM THERMOCOCCUS LITORALIS

Overview

We report the crystallization and structure determination at 1.85 A of the, extracellular, membrane-anchored trehalose/maltose-binding protein (TMBP), in complex with its substrate trehalose. TMBP is the substrate recognition, site of the high-affinity trehalose/maltose ABC transporter of the, hyperthermophilic Archaeon Thermococcus litoralis. In vivo, this protein, is anchored to the membrane, presumably via an N-terminal cysteine lipid, modification. The crystallized protein was N-terminally truncated, resulting in a soluble protein exhibiting the same binding characteristics, as the wild-type protein. The protein shows the characteristic features of, a transport-related, substrate-binding protein and is structurally related, to the maltose-binding protein (MBP) of Escherichia coli. It consists of, two similar lobes, each formed by a parallel beta-sheet flanked by, alpha-helices on both sides. Both are connected by a hinge region, consisting of two antiparallel beta-strands and an alpha-helix. As in MBP, the substrate is bound in the cleft between the lobes by hydrogen bonds, and hydrophobic interactions. However, compared to maltose binding in MBP, direct hydrogen bonding between the substrate and the protein prevails, while apolar contacts are reduced. To elucidate factors contributing to, thermostability, we compared TMBP with its mesophilic counterpart MBP and, found differences known from similar investigations. Specifically, we find, helices that are longer than their structurally equivalent counterparts, and fewer internal cavities.

About this Structure

1EU8 is a Single protein structure of sequence from Thermococcus litoralis with PT, CL and TRE as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of a liganded trehalose/maltose-binding protein from the hyperthermophilic Archaeon Thermococcus litoralis at 1.85 A., Diez J, Diederichs K, Greller G, Horlacher R, Boos W, Welte W, J Mol Biol. 2001 Jan 26;305(4):905-15. PMID:11162101

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