1k87
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(New page: 200px<br /><applet load="1k87" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k87, resolution 2.0Å" /> '''Crystal structure of ...)
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Revision as of 16:49, 20 November 2007
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Crystal structure of E.coli PutA (residues 1-669)
Overview
The PutA flavoprotein from Escherichia coli plays multiple roles in, proline catabolism by functioning as a membrane-associated bi-functional, enzyme and a transcriptional repressor of proline utilization genes. The, human homolog of the PutA proline dehydrogenase (PRODH) domain is critical, in p53-mediated apoptosis and schizophrenia. Here we report the crystal, structure of a 669-residue truncated form of PutA that shows both PRODH, and DNA-binding activities, representing the first structure of a PutA, protein and a PRODH enzyme from any organism. The structure is a, domain-swapped dimer with each subunit comprising three domains: a helical, dimerization arm, a 120-residue domain containing a three-helix bundle, similar to that in the helix-turn-helix superfamily of DNA-binding, proteins and a beta/alpha-barrel PRODH domain with a bound lactate, inhibitor. Analysis of the structure provides insight into the mechanism, of proline oxidation to pyrroline-5-carboxylate, and functional studies of, a mutant protein suggest that the DNA-binding domain is located within the, N-terminal 261 residues of E. coli PutA.
About this Structure
1K87 is a Single protein structure of sequence from Escherichia coli with FAD, 1PE, TRS, LAC and GOL as ligands. Active as Proline dehydrogenase, with EC number 1.5.99.8 Full crystallographic information is available from OCA.
Reference
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein., Lee YH, Nadaraia S, Gu D, Becker DF, Tanner JJ, Nat Struct Biol. 2003 Feb;10(2):109-14. PMID:12514740
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