3OH2

Protein structure of USP from L. major bound to URIDINE-5'-DIPHOSPHATE-GALACTOSE

3OH2 の概要

• エントリーDOI: 10.2210/pdb3oh2/pdb
• 関連するPDBエントリー: 3OGZ 3OH0 3OH1 3OH3 3OH4
• 分子名称: UDP-sugar pyrophosphorylase, GALACTOSE-URIDINE-5'-DIPHOSPHATE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: left handed beta helix, rossmann fold, udp sugar pyrophosphorylase, transferase
• 由来する生物種: Leishmania major
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 71198.33

構造登録者

Dickmanns, A.,Damerow, S.,Neumann, P.,Schulz, E.-C.,Lamerz, A.,Routier, F.,Ficner, R. (登録日: 2010-08-17, 公開日: 2010-11-17, 最終更新日: 2023-09-06)

主引用文献

Dickmanns, A.,Damerow, S.,Neumann, P.,Schulz, E.C.,Lamerz, A.C.,Routier, F.H.,Ficner, R.
Structural basis for the broad substrate range of the UDP-sugar pyrophosphorylase from Leishmania major.
J.Mol.Biol., 405:461-478, 2011

PubMed Abstract: Nucleotide sugars and the enzymes that are responsible for their synthesis are indispensable for the production of complex carbohydrates and, thus, for elaboration of a protective cellular coat for many organisms such as the protozoan parasite Leishmania. These activated sugars are synthesized de novo or derived from salvaged monosaccharides. In addition to UDP-glucose (UDP-Glc) pyrophosphorylase, which catalyzes the formation of UDP-Glc from substrates UTP and glucose-1-phosphate, Leishmania major and plants express a UDP-sugar pyrophosphorylase (USP) that exhibits broad substrate specificity in vitro. The enzyme, likely involved in monosaccharide salvage, preferentially generates UDP-Glc and UDP-galactose, but it may also activate other hexose- or pentose-1-phosphates such as galacturonic acid-1-phosphate or arabinose-1-phosphate. In order to gain insight into structural features governing the differences in substrate specificity, we determined the crystal structure of the L. major USP in the APO-, UTP-, and UDP-sugar-bound conformations. The overall tripartite structure of USP exhibits a significant structural homology to other nucleotidyldiphosphate-glucose pyrophosphorylases. The obtained USP structures reveal the structural rearrangements occurring during the stepwise binding process of the substrates. Moreover, the different product complexes explain the broad substrate specificity of USP, which is enabled by structural changes in the sugar binding region of the active site.

PubMed: 21073876
DOI: 10.1016/j.jmb.2010.10.057

実験手法

X-RAY DIFFRACTION (2.14 Å)