2iy6

File:2iy6.gif

spinqualitylabelsall models 2iy6, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 FLC, NA, CL, MRD and MPD as ligands. Active as 1-pyrroline-5-carboxylate dehydrogenase, with EC number 1.5.1.12 Structure known Active Site: AC1. 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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