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| {{STRUCTURE_1k87| PDB=1k87 | SCENE= }} | | {{STRUCTURE_1k87| PDB=1k87 | SCENE= }} |
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| '''Crystal structure of E.coli PutA (residues 1-669)'''
| | ===Crystal structure of E.coli PutA (residues 1-669)=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12514740}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12514740 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12514740}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Shuttling]] | | [[Category: Shuttling]] |
| [[Category: Transcriptional repressor]] | | [[Category: Transcriptional repressor]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:25:13 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 09:55:46 2008'' |
