1m32

Crystal Structure of 2-aminoethylphosphonate Transaminase

spinqualitylabelsall models 1m32, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1m32 is a 6 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: MSE, PLP, PO4, POA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PHNW_SALTY Involved in phosphonate degradation. 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 PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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