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PDBsum entry 1m32
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Degradation pathway of the phosphonate ciliatine: crystal structure of 2-Aminoethylphosphonate transaminase.
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Authors
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C.C.Chen,
H.Zhang,
A.D.Kim,
A.Howard,
G.M.Sheldrick,
D.Mariano-Dunaway,
O.Herzberg.
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Ref.
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Biochemistry, 2002,
41,
13162-13169.
[DOI no: ]
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PubMed id
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Abstract
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Phosphonates allow certain organisms to thrive in otherwise hostile
environments, and 2-aminoethylphosphonate (AEP) is a precursor of many cellular
phosphonates. AEP transaminase (AEPT) is an enzyme essential to phosphonate
synthesis and degradation pathways. The crystal structure of AEP transaminase
was determined by multiwavelength anomalous diffraction of 66 selenium atoms.
The refined structure at 2.2 A resolution revealed an overall fold and active
site location similar to those of the dimeric, two-domain structure of type I
aminotransferases. The active site contains a cofactor, pyridoxal 5'-phosphate
(PLP), and the product phosphonoacetaldehyde. Comparison with other type I
aminotransferase structures shows that the PLP-protein interactions are
conserved. Modeling of bound substrates and products reveals the structural
basis for AEP recognition and the stereospecificity of proton elimination at the
alpha-carbon and indicates conformational changes along the reaction pathway.
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