1urg

File:1urg.gif

spinqualitylabelsall models 1urg, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Tue Oct 30 13:24:22 2007