2bi3
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RADIATION DAMAGE OF THE SCHIFF BASE IN PHOSPHOSERINE AMINOTRANSFERASE (STRUCTURE D)
OverviewOverview
The X-ray susceptibility of the lysine-pyridoxal-5'-phosphate Schiff base, in Bacillus alcalophilus phosphoserine aminotransferase has been, investigated using crystallographic data collected at 100 K to 1.3 A, resolution, complemented by on-line spectroscopic studies. X-rays induce, deprotonation of the internal aldimine, changes in the Schiff base, conformation, displacement of the cofactor molecule, and disruption of the, Schiff base linkage between pyridoxal-5'-phosphate and the Lys residue., Analysis of the "undamaged" structure reveals a significant chemical, strain on the internal aldimine bond that leads to a pronounced, geometrical distortion of the cofactor. However, upon crystal exposure to, the X-rays, the strain and distortion are relaxed and eventually, diminished when the ... [(full description)]
About this StructureAbout this Structure
2BI3 is a [Single protein] structure of sequence from [Bacillus alcalophilus] with MG, CL, PLP, 1PE and PEG as [ligands]. Active as [[1]], with EC number [2.6.1.52]. Full crystallographic information is available from [OCA].
ReferenceReference
Strain relief at the active site of phosphoserine aminotransferase induced by radiation damage., Dubnovitsky AP, Ravelli RB, Popov AN, Papageorgiou AC, Protein Sci. 2005 Jun;14(6):1498-507. Epub 2005 May 9. PMID:15883191
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