1k87
From Proteopedia
(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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| - | [[Image:1k87.gif|left|200px]]<br /><applet load="1k87" size=" | + | [[Image:1k87.gif|left|200px]]<br /><applet load="1k87" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1k87, resolution 2.0Å" /> | caption="1k87, resolution 2.0Å" /> | ||
'''Crystal structure of E.coli PutA (residues 1-669)'''<br /> | '''Crystal structure of E.coli PutA (residues 1-669)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The PutA flavoprotein from Escherichia coli plays multiple roles in | + | 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== | ==About this Structure== | ||
| - | 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:// | + | 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 <scene name='pdbligand=FAD:'>FAD</scene>, <scene name='pdbligand=1PE:'>1PE</scene>, <scene name='pdbligand=TRS:'>TRS</scene>, <scene name='pdbligand=LAC:'>LAC</scene> and <scene name='pdbligand=GOL:'>GOL</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1K87 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Proline dehydrogenase]] | [[Category: Proline dehydrogenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Becker, D | + | [[Category: Becker, D F.]] |
| - | [[Category: Lee, Y | + | [[Category: Lee, Y H.]] |
[[Category: Nadaria, S.]] | [[Category: Nadaria, S.]] | ||
| - | [[Category: Tanner, J | + | [[Category: Tanner, J J.]] |
[[Category: 1PE]] | [[Category: 1PE]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
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[[Category: multi-functional protein; proline dehydrogenase; transcriptional repressor; shuttling; dimer]] | [[Category: multi-functional protein; proline dehydrogenase; transcriptional repressor; shuttling; dimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:09 2008'' |
Revision as of 11:31, 21 February 2008
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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 , , , and 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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