2D2I

Crystal Structure of NADP-Dependent Glyceraldehyde-3-Phosphate Dehydrogenase from Synechococcus Sp. complexed with Nadp+

2D2I の概要

• エントリーDOI: 10.2210/pdb2d2i/pdb
• 分子名称: glyceraldehyde 3-phosphate dehydrogenase, SULFATE ION, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: glyceraldehyde 3-phosphate dehydrogenase, rossmann fold, protein-nadp+ complex, oxidoreductase
• 由来する生物種: Synechococcus sp.
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 253916.60

構造登録者

Kitatani, T.,Nakamura, Y.,Wada, K.,Kinoshita, T.,Tamoi, M.,Shigeoka, S.,Tada, T. (登録日: 2005-09-09, 公開日: 2006-07-11, 最終更新日: 2024-03-13)

主引用文献

Kitatani, T.,Nakamura, Y.,Wada, K.,Kinoshita, T.,Tamoi, M.,Shigeoka, S.,Tada, T.
Structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC7942 complexed with NADP
Acta Crystallogr.,Sect.F, 62:315-319, 2006

PubMed Abstract: The crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (NADP-GAPDH) from Synechococcus PCC 7942 (S. 7942) in complex with NADP was solved by molecular replacement and refined to an R factor of 19.1% and a free R factor of 24.0% at 2.5 A resolution. The overall structure of NADP-GAPDH from S. 7942 was quite similar to those of other bacterial and eukaryotic GAPDHs. The nicotinamide ring of NADP, which is involved in the redox reaction, was oriented toward the catalytic site. The 2'-phosphate O atoms of NADP exhibited hydrogen bonds to the hydroxyl groups of Ser194 belonging to the S-loop and Thr37. These residues are therefore considered to be essential in the discrimination between NADP and NAD molecules. The C-terminal region was estimated to have an extremely flexible conformation and to play an important role in the formation of the supramolecular complex phosphoribulokinase (PRK)-regulatory peptide (CP12)-GAPDH, which regulates enzyme activities.

PubMed: 16582475
DOI: 10.1107/S1744309106007378

実験手法

X-RAY DIFFRACTION (2.5 Å)