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, ... [(full description)]

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]], with EC number [1.5.1.12]. 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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