1m32
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(New page: 200px<br /><applet load="1m32" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m32, resolution 2.2Å" /> '''Crystal Structure of ...)
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Revision as of 18:59, 20 November 2007
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Crystal Structure of 2-aminoethylphosphonate Transaminase
Overview
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.
About this Structure
1M32 is a Single protein structure of sequence from Salmonella typhimurium with PO4, PLP and POA as ligands. Active as 2-aminoethylphosphonate--pyruvate transaminase, with EC number 2.6.1.37 Full crystallographic information is available from OCA.
Reference
Degradation pathway of the phosphonate ciliatine: crystal structure of 2-aminoethylphosphonate transaminase., Chen CC, Zhang H, Kim AD, Howard A, Sheldrick GM, Mariano-Dunaway D, Herzberg O, Biochemistry. 2002 Nov 5;41(44):13162-9. PMID:12403617
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