2BJK

Crystal Analysis of 1-Pyrroline-5-Carboxylate Dehydrogenase from Thermus with bound NAD and citrate.

Summary for 2BJK

• Entry DOI: 10.2210/pdb2bjk/pdb
• Related: 2BHP 2BHQ 2BJA
• Descriptor: 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, CITRATE ANION, ... (7 entities in total)
• Functional Keywords: 1-pyrroline-5-carboxylate, dehyrogenase, oxidoreductase
• Biological source: THERMUS THERMOPHILUS
• Total number of polymer chains: 2
• Total formula weight: 117067.33

Authors

Inagaki, E.,Tahirov, T.H. (deposition date: 2005-02-04, release date: 2006-03-09, Last modification date: 2023-12-13)

Primary citation

Inagaki, E.,Ohshima, N.,Takahashi, H.,Kuroishi, C.,Yokoyama, S.,Tahirov, T.H.
Crystal Structure of Thermus Thermophilus Delta(1)- Pyrroline-5-Carboxylate Dehydrogenase.
J.Mol.Biol., 362:490-, 2006

PubMed Abstract: 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.

PubMed: 16934832
DOI: 10.1016/J.JMB.2006.07.048

Experimental method

X-RAY DIFFRACTION (1.4 Å)