2bie: Difference between revisions

Revision as of 07:24, 28 July 2008

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File:2bie.png

Template:STRUCTURE 2bie

RADIATION DAMAGE OF THE SCHIFF BASE IN PHOSPHOSERINE AMINOTRANSFERASE (STRUCTURE H)RADIATION DAMAGE OF THE SCHIFF BASE IN PHOSPHOSERINE AMINOTRANSFERASE (STRUCTURE H)

Template:ABSTRACT PUBMED 15883191

About this StructureAbout this Structure

2BIE is a Single protein structure of sequence from Bacillus alcalophilus. 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''RADIATION DAMAGE OF THE SCHIFF BASE IN PHOSPHOSERINE AMINOTRANSFERASE (STRUCTURE H)'''
+===RADIATION DAMAGE OF THE SCHIFF BASE IN PHOSPHOSERINE AMINOTRANSFERASE (STRUCTURE H)===
-==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 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15883191}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15883191 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15883191}}
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 [[Category: Radiation damage]]
 [[Category: Transferase]]
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