1KY8

Crystal Structure of the Non-phosphorylating glyceraldehyde-3-phosphate Dehydrogenase

1KY8 の概要

• エントリーDOI: 10.2210/pdb1ky8/pdb
• 分子名称: glyceraldehyde-3-phosphate dehydrogenase, SODIUM ION, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: gapn, aldh, oxidoreductase
• 由来する生物種: Thermoproteus tenax
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54924.67

構造登録者

Pohl, E.,Brunner, N.,Wilmanns, M.,Hensel, R. (登録日: 2002-02-04, 公開日: 2003-02-04, 最終更新日: 2024-02-14)

主引用文献

Pohl, E.,Brunner, N.,Wilmanns, M.,Hensel, R.
The Crystal Structure of the Allosteric Non-phosphorylating glyceraldehyde-3-phosphate Dehydrogenase from the Hyperthermophilic Archaeum Thermoproteus tenax
J.Biol.Chem., 277:19938-19945, 2002

PubMed Abstract: The NAD(+)-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) from the hyperthermophilic archaeum Thermoproteus tenax represents an archaeal member of the diverse superfamily of aldehyde dehydrogenases (ALDHs). GAPN catalyzes the irreversible oxidation of d-glyceraldehyde 3-phosphate to 3-phosphoglycerate. In this study, we present the crystal structure of GAPN in complex with its natural inhibitor NADP(+) determined by multiple anomalous diffraction methods. The structure was refined to a resolution of 2.4 A with an R-factor of 0.21. The overall fold of GAPN is similar to the structures of ALDHs described previously, consisting of three domains: a nucleotide-binding domain, a catalytic domain, and an oligomerization domain. Local differences in the active site are responsible for substrate specificity. The inhibitor NADP(+) binds at an equivalent site to the cosubstrate-binding site of other ALDHs and blocks the enzyme in its inactive state, possibly preventing the transition to the active conformation. Structural comparison between GAPN from the hyperthermophilic T. tenax and homologs of mesophilic organisms establishes several characteristics of thermostabilization. These include protection against heat-induced covalent modifications by reducing and stabilizing labile residues, a decrease in number and volume of empty cavities, an increase in beta-strand content, and a strengthening of subunit contacts by ionic and hydrophobic interactions.

PubMed: 11842090
DOI: 10.1074/jbc.M112244200

実験手法

X-RAY DIFFRACTION (2.4 Å)