1w3u
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(New page: 200px<br /> <applet load="1w3u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w3u, resolution 1.50Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 16:10, 29 October 2007
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CRYSTAL STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM BACILLUS CIRCULANS VAR. ALKALOPHILUS
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
1W3U is a [Single protein] structure of sequence from [Bacillus circulans] with PLP and GOL as [ligands]. Active as [[1]], with EC number [2.6.1.52]. 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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