2bi9: Difference between revisions
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==Overview== | ==Overview== | ||
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 ... | 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 total absorbed dose has exceeded 4.7 x 10(6) Ggamma., Our data provide new insights into the enzymatic activation of, pyridoxal-5'-phosphate and suggest that special care should be taken while, using macromolecular crystallography to study details in strained active, sites. | ||
==About this Structure== | ==About this Structure== | ||
2BI9 is a | 2BI9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_alcalophilus Bacillus alcalophilus] with MG, CL, PLP, 1PE and PEG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoserine_transaminase Phosphoserine transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.52 2.6.1.52] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BI9 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
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