2iy6: Difference between revisions
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==Overview== | ==Overview== | ||
Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDh) plays an important | 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== | ==About this Structure== | ||
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[[Category: Inagaki, E.]] | [[Category: Inagaki, E.]] | ||
[[Category: Nishio, M.]] | [[Category: Nishio, M.]] | ||
[[Category: RSGI, RIKEN | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] | ||
[[Category: Sakamoto, K.]] | [[Category: Sakamoto, K.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:57:26 2008'' | ||
Revision as of 18:57, 21 February 2008
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1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE FROM THERMUS WITH BOUND CITRATE
OverviewOverview
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 StructureAbout this Structure
2IY6 is a Single protein structure of sequence from Thermus thermophilus with , , , and as ligands. Active as 1-pyrroline-5-carboxylate dehydrogenase, with EC number 1.5.1.12 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- 1-pyrroline-5-carboxylate dehydrogenase
- Single protein
- Thermus thermophilus
- Inagaki, E.
- Nishio, M.
- RSGI, RIKEN Structural Genomics/Proteomics Initiative.
- Sakamoto, K.
- Yokoyama, S.
- CL
- FLC
- MPD
- MRD
- NA
- 1-pyrroline-5-carboxylate
- Citrate
- Dehyrogenase
- Oxidoreductase
- Riken structural genomics/proteomics initiative
- Rsgi
- Structural genomics