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| [[Image:2bhp.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2bhp| PDB=2bhp | SCENE= }} | | {{STRUCTURE_2bhp| PDB=2bhp | SCENE= }} |
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| '''CRYSTAL ANALYSIS OF 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE FROM THERMUS WITH BOUND NAD.'''
| | ===CRYSTAL ANALYSIS OF 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE FROM THERMUS WITH BOUND NAD.=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16934832}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16934832 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16934832}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Rsgi]] | | [[Category: Rsgi]] |
| [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:18:14 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:12:04 2008'' |