2bie: Difference between revisions
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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)== | ||
<StructureSection load='2bie' size='340' side='right' caption='[[2bie]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='2bie' size='340' side='right'caption='[[2bie]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2bie]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27647 Atcc 27647]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BIE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BIE FirstGlance]. <br> | <table><tr><td colspan='2'>[[2bie]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27647 Atcc 27647]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BIE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BIE FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 27647]] | [[Category: Atcc 27647]] | ||
[[Category: Large Structures]] | |||
[[Category: Phosphoserine transaminase]] | [[Category: Phosphoserine transaminase]] | ||
[[Category: Dubnovitsky, A P]] | [[Category: Dubnovitsky, A P]] | ||
Revision as of 10:10, 23 May 2019
Radiation damage of the Schiff base in phosphoserine aminotransferase (structure H)Radiation damage of the Schiff base in phosphoserine aminotransferase (structure H)
Structural highlights
Function[SERC_BACAO] Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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