1EYR

Structure of a sialic acid activating synthetase, CMP acylneuraminate synthetase in the presence and absence of CDP

1EYR の概要

• エントリーDOI: 10.2210/pdb1eyr/pdb
• 関連するPDBエントリー: 1EZI
• 分子名称: CMP-N-ACETYLNEURAMINIC ACID SYNTHETASE, CYTIDINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: synthetase, sialic acid, cdp, acylneuraminate, transferase
• 由来する生物種: Neisseria meningitidis
• 細胞内の位置: Cytoplasm: P0A0Z8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51116.12

構造登録者

Mosimann, S.C.,Gilbert, M.,Dombrowski, D.,Wakarchuk, W.,Strynadka, N.C. (登録日: 2000-05-08, 公開日: 2001-02-14, 最終更新日: 2024-11-20)

主引用文献

Mosimann, S.C.,Gilbert, M.,Dombroswki, D.,To, R.,Wakarchuk, W.,Strynadka, N.C.
Structure of a sialic acid-activating synthetase, CMP-acylneuraminate synthetase in the presence and absence of CDP.
J.Biol.Chem., 276:8190-8196, 2001

PubMed Abstract: The x-ray crystallographic structure of selenomethionyl cytosine-5'-monophosphate-acylneuraminate synthetase (CMP-NeuAc synthetase) from Neisseria meningitidis has been determined at 2.0-A resolution using multiple-wavelength anomalous dispersion phasing, and a second structure, in the presence of the substrate analogue CDP, has been determined at 2.2-A resolution by molecular replacement. This work identifies the active site residues for this class of enzyme for the first time. The detailed interactions between the enzyme and CDP within the mononucleotide-binding pocket are directly observed, and the acylneuraminate-binding pocket has also been identified. A model of acylneuraminate bound to CMP-NeuAc synthetase has been constructed and provides a structural basis for understanding the mechanism of production of "activated" sialic acids. Sialic acids are key saccharide components on the surface of mammalian cells and can be virulence factors in a variety of bacterial species (e.g. Neisseria, Haemophilus, group B streptococci, etc.). As such, the identification of the bacterial CMP-NeuAc synthetase active site can serve as a starting point for rational drug design strategies.

PubMed: 11113120
DOI: 10.1074/jbc.M007235200

実験手法

X-RAY DIFFRACTION (2.2 Å)