1w23

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spinqualitylabelsall models 1w23, resolution 1.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM BACILLUS ALCALOPHILUS

Overview

The crystal structure of the vitamin B(6)-dependent enzyme phosphoserine, aminotransferase from the obligatory alkaliphile Bacillus alcalophilus has, been determined at 1.08 A resolution. The model was refined to an R-factor, of 11.7% (R(free) = 13.9%). The enzyme displays a narrow pH optimum of, enzymatic activity at pH 9.0. The final structure was compared to the, previously reported structure of the mesophilic phosphoserine, aminotransferase from Escherichia coli and to that of phosphoserine, aminotransferase from a facultative alkaliphile, Bacillus circulans subsp., alkalophilus. All three enzymes are homodimers with each monomer, comprising a two-domain architecture. Despite the high structural, similarity, the alkaliphilic representatives possess a set of distinctive, structural ... [(full description)]

About this Structure

1W23 is a [Single protein] structure of sequence from [Bacillus alcalophilus] with MG, CL, PGE, PLP, EPE, PEG and GOL as [ligands]. Active as [Phosphoserine transaminase], with EC number [2.6.1.52]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of phosphoserine aminotransferase from Bacillus alcalophilus., Dubnovitsky AP, Kapetaniou EG, Papageorgiou AC, Protein Sci. 2005 Jan;14(1):97-110. PMID:15608117

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