3daa: Difference between revisions

Revision as of 15:20, 28 July 2008

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File:3daa.png

Template:STRUCTURE 3daa

CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE INACTIVATED BY PYRIDOXYL-D-ALANINECRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE INACTIVATED BY PYRIDOXYL-D-ALANINE

Template:ABSTRACT PUBMED 9538014

About this StructureAbout this Structure

3DAA is a Single protein structure of sequence from Bacillus sp.. Full crystallographic information is available from OCA.

ReferenceReference

Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase., Peisach D, Chipman DM, Van Ophem PW, Manning JM, Ringe D, Biochemistry. 1998 Apr 7;37(14):4958-67. PMID:9538014

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 {{STRUCTURE_3daa|  PDB=3daa  |  SCENE=  }}
-'''CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE INACTIVATED BY PYRIDOXYL-D-ALANINE'''
+===CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE INACTIVATED BY PYRIDOXYL-D-ALANINE===
-==Overview==
+<!--
-The three-dimensional structures of two forms of the D-amino acid aminotransferase (D-aAT) from Bacillus sp. YM-1 have been determined crystallographically: the pyridoxal phosphate (PLP) form and a complex with the reduced analogue of the external aldimine, N-(5'-phosphopyridoxyl)-d-alanine (PPDA). Together with the previously reported pyridoxamine phosphate form of the enzyme [Sugio et al. (1995) Biochemistry 34, 9661], these structures allow us to describe the pathway of the enzymatic reaction in structural terms. A major determinant of the enzyme's stereospecificity for D-amino acids is a group of three residues (Tyr30, Arg98, and His100, with the latter two contributed by the neighboring subunit) forming four hydrogen bonds to the substrate alpha-carboxyl group. The replacement by hydrophobic groups of the homologous residues of the branched chain L-amino acid aminotransferase (which has a similar fold) could explain its opposite stereospecificity. As in L-aspartate aminotransferase (L-AspAT), the cofactor in D-aAT tilts (around its phosphate group and N1 as pivots) away from the catalytic lysine 145 and the protein face in the course of the reaction. Unlike L-AspAT, D-aAT shows no other significant conformational changes during the reaction.
+The line below this paragraph, {{ABSTRACT_PUBMED_9538014}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9538014 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9538014}}
 ==About this Structure==
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 [[Category: Pyridoxal phosphate]]
 [[Category: Transaminase]]
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