1k87: Difference between revisions
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New page: left|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'' | ||
