3KO8

Crystal Structure of UDP-galactose 4-epimerase

3KO8 の概要

• エントリーDOI: 10.2210/pdb3ko8/pdb
• 分子名称: NAD-dependent epimerase/dehydratase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: isomerase, udp-galactose 4-epimerase
• 由来する生物種: Pyrobaculum calidifontis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35154.92

構造登録者

Sakuraba, H.,Kawai, T.,Yoneda, K.,Ohshima, T. (登録日: 2009-11-13, 公開日: 2010-11-17, 最終更新日: 2023-11-01)

主引用文献

Sakuraba, H.,Kawai, T.,Yoneda, K.,Ohshima, T.
Crystal structure of UDP-galactose 4-epimerase from the hyperthermophilic archaeon Pyrobaculum calidifontis
Arch.Biochem.Biophys., 512:126-134, 2011

PubMed Abstract: The crystal structure of a highly thermostable UDP-galactose 4-epimerase (GalE) from the hyperthermophilic archaeon Pyrobaculum calidifontis was determined at a resolution of 1.8Å. The asymmetric unit contained one subunit, and the functional dimer was generated by a crystallographic two-fold axis. Each monomer consisted of a Rossmann-fold domain with NAD bound and a carboxyl terminal domain. The overall structure of P. calidifontis GalE showed significant similarity to the structures of the GalEs from Escherichia coli, human and Trypanosoma brucei. However, the sizes of several surface loops were markedly smaller in P. calidifontis GalE than the corresponding loops in the other enzymes. Structural comparison revealed that the presence of an extensive hydrophobic interaction at the subunit interface is likely the main factor contributing to the hyperthermostability of the P. calidifontis enzyme. Within the NAD-binding site of P. calidifontis GalE, a loop (NAD-binding loop) tightly holds the adenine ribose moiety of NAD. Moreover, a deletion mutant lacking this loop bound NAD in a loose, reversible manner. Thus the presence of the NAD-binding loop in GalE is largely responsible for preventing the release of the cofactor from the holoenzyme.

PubMed: 21645492
DOI: 10.1016/j.abb.2011.05.013

実験手法

X-RAY DIFFRACTION (1.8 Å)