2c0r

File:2c0r.gif

spinqualitylabelsall models 2c0r, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM BACILLUS CIRCULANS VAR. ALKALOPHILUS AT PH 8.5

OverviewOverview

pH is one of the key parameters that affect the stability and function of, proteins. We have studied the effect of pH on the, pyridoxal-5'-phosphate-dependent enzyme phosphoserine aminotransferase, produced by the facultative alkaliphile Bacillus circulans ssp., alkalophilus using thermodynamic and crystallographic analysis. Enzymatic, activity assay showed that the enzyme has maximum activity at pH 9.0 and, relative activity less than 10% at pH 7.0. Differential scanning, calorimetry and circular dichroism experiments revealed variations in the, stability and denaturation profiles of the enzyme at different pHs. Most, importantly, release of pyridoxal-5'-phosphate and protein thermal, denaturation were found to occur simultaneously at pH 6.0 in contrast to, pH 8.5 where denaturation ... [(full description)]

About this StructureAbout this Structure

2C0R is a [Single protein] structure of sequence from [Bacillus circulans] with PLP as [ligand]. Active as [Phosphoserine transaminase], with EC number [2.6.1.52]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

Effect of pH on the structure and stability of Bacillus circulans ssp. alkalophilus phosphoserine aminotransferase: thermodynamic and crystallographic studies., Kapetaniou EG, Thanassoulas A, Dubnovitsky AP, Nounesis G, Papageorgiou AC, Proteins. 2006 Jun 1;63(4):742-53. PMID:16532449

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