2AHR

Crystal Structures of 1-Pyrroline-5-Carboxylate Reductase from Human Pathogen Streptococcus pyogenes

2AHR の概要

• エントリーDOI: 10.2210/pdb2ahr/pdb
• 関連するPDBエントリー: 1YQG 2AG8
• 分子名称: putative pyrroline carboxylate reductase, SODIUM ION, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: 1-pyrroline-5-carboxylate reductase, pyrroline-5-carboxylate reductase, pyrroline reductase, proline biosynthesis, nad(p)binding protein, rossmann fold, doain swapping, human pathogen, streptococcus pyogenes, structural genomics, mcsg, psi, protein structure initiative, midwest center for structural genomics, oxidoreductase
• 由来する生物種: Streptococcus pyogenes
• 細胞内の位置: Cytoplasm : Q9A1S9
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 143728.36

構造登録者

Nocek, B.,Lezondra, L.,Holzle, D.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2005-07-28, 公開日: 2005-09-13, 最終更新日: 2024-11-13)

主引用文献

Nocek, B.,Chang, C.,Li, H.,Lezondra, L.,Holzle, D.,Collart, F.,Joachimiak, A.
Crystal Structures of Delta(1)-Pyrroline-5-carboxylate Reductase from Human Pathogens Neisseria meningitides and Streptococcus pyogenes
J.Mol.Biol., 354:91-106, 2005

PubMed Abstract: L-proline is an amino acid that plays an important role in proteins uniquely contributing to protein folding, structure, and stability, and this amino acid serves as a sequence-recognition motif. Proline biosynthesis can occur via two pathways, one from glutamate and the other from arginine. In both pathways, the last step of biosynthesis, the conversion of delta1-pyrroline-5-carboxylate (P5C) to L-proline, is catalyzed by delta1-pyrroline-5-carboxylate reductase (P5CR) using NAD(P)H as a cofactor. We have determined the first crystal structure of P5CR from two human pathogens, Neisseria meningitides and Streptococcus pyogenes, at 2.0 angstroms and 2.15 angstroms resolution, respectively. The catalytic unit of P5CR is a dimer composed of two domains, but the biological unit seems to be species-specific. The N-terminal domain of P5CR is an alpha/beta/alpha sandwich, a Rossmann fold. The C-terminal dimerization domain is rich in alpha-helices and shows domain swapping. Comparison of the native structure of P5CR to structures complexed with L-proline and NADP+ in two quite different primary sequence backgrounds provides unique information about key functional features: the active site and the catalytic mechanism. The inhibitory L-proline has been observed in the crystal structure.

PubMed: 16233902
DOI: 10.1016/j.jmb.2005.08.036

実験手法

X-RAY DIFFRACTION (2.15 Å)