1TZF

X-ray Crystal Structure of alpha-D-glucose-1-phosphate cytidylyltransferase from Salmonella typhi

1TZF の概要

• エントリーDOI: 10.2210/pdb1tzf/pdb
• 分子名称: Glucose-1-phosphate cytidylyltransferase, MAGNESIUM ION, [CYTIDINE-5'-PHOSPHATE]-BETA-GLUCOSYL-PHOSPHORIC ACID ESTER, ... (4 entities in total)
• 機能のキーワード: nucleotidyltransferase; mixed alpha/beta fold, transferase
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhi
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29793.22

構造登録者

Koropatkin, N.M.,Holden, H.M. (登録日: 2004-07-09, 公開日: 2004-09-07, 最終更新日: 2024-02-14)

主引用文献

Koropatkin, N.M.,Holden, H.M.
Molecular structure of alpha-D-glucose-1-phosphate cytidylyltransferase from Salmonella typhi
J.Biol.Chem., 279:44023-44029, 2004

PubMed Abstract: Dideoxysugars, which display biological activities ranging from mediating cell-cell interactions to serving as components in some antibiotics, are synthesized in various organisms via complex biochemical pathways that begin with the attachment of alpha-D-glucose 1-phosphate to either CTP or dTTP. Here we describe the three-dimensional structure of the alpha-D-glucose-1-phosphate cytidylyltransferase from Salmonella typhi, which catalyzes the first step in the production of CDP-tyvelose. For this investigation, the enzyme was crystallized in the presence of its product, CDP-glucose. In contrast to previous reports, the enzyme exists as a fully integrated hexamer with 32-point group symmetry. Each subunit displays a "bird-like" appearance with the "body" composed predominantly of a seven-stranded mixed beta-sheet and the two "wings" formed by beta-hairpin motifs. These two wings mediate subunit-subunit interactions along the 3-fold and 2-fold rotational axes, respectively. The six active sites of the hexamer are situated between the subunits related by the 2-fold rotational axes. CDP-glucose is anchored to the protein primarily by hydrogen bonds with backbone carbonyl oxygens and peptidic NH groups. The side chains of Arg111 and Asn188 from one subunit and Glu178 and Lys179 from the second subunit are also involved in hydrogen bonding with the ligand. The topology of the main core domain bears striking similarity to that observed for glucose-1-phosphate thymidylyltransferase and 4-diphosphocytidyl-2-C-methylerythritol synthetase.

PubMed: 15292268
DOI: 10.1074/jbc.M407755200

実験手法

X-RAY DIFFRACTION (2.1 Å)