3SC6

2.65 Angstrom resolution crystal structure of dTDP-4-dehydrorhamnose reductase (rfbD) from Bacillus anthracis str. Ames in complex with NADP

3SC6 の概要

• エントリーDOI: 10.2210/pdb3sc6/pdb
• 分子名称: dTDP-4-dehydrorhamnose reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: dtdp-4-dehydrorhamnose reductase, rfbd, structural genomics, infectious diseases, bacillus anthracis str. ames, rhamnose biosynthetic pathway, center for structural genomics of infectious diseases, csgid, rossmann fold, catalyzes formation of dtdp-4-dehydro-6-deoxy-l-mannose, nadph and h+ from dtdp-6-deoxy-l-mannose and nadp+, oxidoreductase
• 由来する生物種: Bacillus anthracis (anthrax, anthrax bacterium)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 202420.32

構造登録者

Halavaty, A.S.,Kuhn, M.,Shuvalova, L.,Minasov, G.,Peterson, S.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2011-06-07, 公開日: 2011-06-22, 最終更新日: 2023-09-13)

主引用文献

Law, A.,Stergioulis, A.,Halavaty, A.S.,Minasov, G.,Anderson, W.F.,Kuhn, M.L.
Structure of the Bacillus anthracis dTDP-L-rhamnose-biosynthetic enzyme dTDP-4-dehydrorhamnose reductase (RfbD).
Acta Crystallogr F Struct Biol Commun, 73:644-650, 2017

PubMed Abstract: Bacillus anthracis is the causative agent of the deadly disease Anthrax. Its use in bioterrorism and its ability to re-emerge have brought renewed interest in this organism. B. anthracis is a Gram-positive bacterium that adds L-rhamnose to its cell-wall polysaccharides using the activated donor dTDP-β-L-rhamnose. The enzymes involved in the biosynthesis of the activated donor are absent in humans, which make them ideal targets for therapeutic development to combat pathogens. Here, the 2.65 Å resolution crystal structure of the fourth enzyme in the dTDP-β-L-rhamnose-biosynthetic pathway from B. anthracis, dTDP-4-dehydro-β-L-rhamnose reductase (RfbD), is presented in complex with NADP. This enzyme catalyzes the reduction of dTDP-4-dehydro-β-L-rhamnose to dTDP-β-L-rhamnose. Although the protein was co-crystallized in the presence of Mg, the protein lacks the conserved residues that coordinate Mg.

PubMed: 29199984
DOI: 10.1107/S2053230X17015746

実験手法

X-RAY DIFFRACTION (2.65 Å)