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1daa
From Proteopedia
Revision as of 06:30, 4 September 2014 by OCA (Talk | contribs)
1daa is a 2 chain structure with sequence from Bacillus sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The three-dimensional structure of D-amino acid aminotransferase (D-AAT) in the pyridoxamine phosphate form has been determined crystallographically. The fold of this pyridoxal phosphate (PLP)-containing enzyme is completely different from those of any of the other enzymes that utilize PLP as part of their mechanism and whose structures are known. However, there are some striking similarities between the active sites of D-AAT and the corresponding enzyme that transaminates L-amino acids, L-aspartate aminotransferase. These similarities represent convergent evolution to a common solution of the problem of enforcing transamination chemistry on the PLP cofactor. Implications of these similarities are discussed in terms of their possible roles in the stabilization of intermediates of a transamination reaction. In addition, sequence similarity between D-AAT and branched chain L-amino acid aminotransferase suggests that this latter enzyme will also have a fold similar to that of D-AAT.
Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity.,Sugio S, Petsko GA, Manning JM, Soda K, Ringe D Biochemistry. 1995 Aug 1;34(30):9661-9. PMID:7626635[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Sugio S, Petsko GA, Manning JM, Soda K, Ringe D. Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity. Biochemistry. 1995 Aug 1;34(30):9661-9. PMID:7626635
