1urs

From Proteopedia

Revision as of 11:20, 30 October 2007

X-RAY STRUCTURES OF THE MALTOSE-MALTODEXTRIN BINDING PROTEIN OF THE THERMOACIDOPHILIC BACTERIUM ALICYCLOBACILLUS ACIDOCALDARIUS

Overview

Maltose-binding proteins act as primary receptors in bacterial transport, and chemotaxis systems. We report here crystal structures of the, thermoacidostable maltose-binding protein from Alicyclobacillus, acidocaldarius, and explore its modes of binding to maltose and, maltotriose. Further, comparison with the structures of related proteins, from Escherichia coli (a mesophile), and two hyperthermophiles (Pyrococcus, furiosus and Thermococcus litoralis) allows an investigation of the basis, of thermo- and acidostability in this family of proteins.The, thermoacidophilic protein has fewer charged residues than the other three, structures, which is compensated by an increase in the number of polar, residues. Although the content of acidic and basic residues is, approximately equal, more basic ... [(full description)]

About this Structure

1URS is a [Single protein] structure of sequence from [Alicyclobacillus acidocaldarius] with MLR as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

X-ray structures of the maltose-maltodextrin-binding protein of the thermoacidophilic bacterium Alicyclobacillus acidocaldarius provide insight into acid stability of proteins., Schafer K, Magnusson U, Scheffel F, Schiefner A, Sandgren MO, Diederichs K, Welte W, Hulsmann A, Schneider E, Mowbray SL, J Mol Biol. 2004 Jan 2;335(1):261-74. PMID:14659755

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