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| - | [[Image:1k87.gif|left|200px]]<br /><applet load="1k87" size="450" color="white" frame="true" align="right" spinBox="true" | + | #REDIRECT [[4o8a]] This PDB entry is obsolete and replaced by 4o8a |
| - | caption="1k87, resolution 2.0Å" />
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| - | '''Crystal structure of E.coli PutA (residues 1-669)'''<br />
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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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with FAD, 1PE, TRS, LAC and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:56:25 2007''
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