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| - | [[Image:1k87.gif|left|200px]] | + | #REDIRECT [[4o8a]] This PDB entry is obsolete and replaced by 4o8a |
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| - | {{Structure
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| - | |PDB= 1k87 |SIZE=350|CAPTION= <scene name='initialview01'>1k87</scene>, resolution 2.0Å
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| - | |SITE=
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| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=LAC:LACTIC+ACID'>LAC</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Proline_dehydrogenase Proline dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.99.8 1.5.99.8]
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| - | |GENE=
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| - | }}
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| - | '''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.
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| - | ==About this Structure==
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| - | 1K87 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K87 OCA].
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| - | ==Reference==
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| - | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12514740 12514740]
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| - | [[Category: Escherichia coli]]
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| - | [[Category: Proline dehydrogenase]]
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| - | [[Category: Single protein]]
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| - | [[Category: Becker, D F.]]
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| - | [[Category: Lee, Y H.]]
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| - | [[Category: Nadaria, S.]]
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| - | [[Category: Tanner, J J.]]
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| - | [[Category: 1PE]]
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| - | [[Category: FAD]]
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| - | [[Category: GOL]]
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| - | [[Category: LAC]]
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| - | [[Category: TRS]]
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| - | [[Category: multi-functional protein; proline dehydrogenase; transcriptional repressor; shuttling; dimer]]
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:13:50 2008''
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