2bjk
From Proteopedia
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|PDB= 2bjk |SIZE=350|CAPTION= <scene name='initialview01'>2bjk</scene>, resolution 1.40Å | |PDB= 2bjk |SIZE=350|CAPTION= <scene name='initialview01'>2bjk</scene>, resolution 1.40Å | ||
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/1-pyrroline-5-carboxylate_dehydrogenase 1-pyrroline-5-carboxylate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.12 1.5.1.12] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/1-pyrroline-5-carboxylate_dehydrogenase 1-pyrroline-5-carboxylate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.12 1.5.1.12] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bjk OCA], [http://www.ebi.ac.uk/pdbsum/2bjk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bjk RCSB]</span> | ||
}} | }} | ||
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[[Category: Inagaki, E.]] | [[Category: Inagaki, E.]] | ||
[[Category: Tahirov, T H.]] | [[Category: Tahirov, T H.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: FLC]] | ||
| - | [[Category: MPD]] | ||
| - | [[Category: MRD]] | ||
| - | [[Category: NAD]] | ||
[[Category: 1-pyrroline-5-carboxylate]] | [[Category: 1-pyrroline-5-carboxylate]] | ||
[[Category: dehyrogenase]] | [[Category: dehyrogenase]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:07:20 2008'' |
Revision as of 23:07, 30 March 2008
| |||||||
| , resolution 1.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , | ||||||
| Activity: | 1-pyrroline-5-carboxylate dehydrogenase, with EC number 1.5.1.12 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL ANALYSIS OF 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE FROM THERMUS WITH BOUND NAD AND CITRATE.
Overview
Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDh) plays an important role in the metabolic pathway from proline to glutamate. It irreversibly catalyzes the oxidation of glutamate-gamma-semialdehyde, the product of the non-enzymatic hydrolysis of Delta(1)-pyrroline-5-carboxylate, into glutamate with the reduction of NAD(+) into NADH. We have confirmed the P5CDh activity of the Thermus thermophilus protein TT0033 (TtP5CDh), and determined the crystal structure of the enzyme in the ligand-free form at 1.4 A resolution. To investigate the structural basis of TtP5CDh function, the TtP5CDh structures with NAD(+), with NADH, and with its product glutamate were determined at 1.8 A, 1.9 A, and 1.4 A resolution, respectively. The solved structures suggest an overall view of the P5CDh catalytic mechanism and provide insights into the P5CDh deficiencies in the case of the human type II hyperprolinemia.
About this Structure
2BJK is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Crystal structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase., Inagaki E, Ohshima N, Takahashi H, Kuroishi C, Yokoyama S, Tahirov TH, J Mol Biol. 2006 Sep 22;362(3):490-501. Epub 2006 Jul 29. PMID:16934832
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