5TGD

Crystal structure of FolM Alternative dihydrofolate reductase 1 from Brucella suis in complex with NADP

5TGD の概要

• エントリーDOI: 10.2210/pdb5tgd/pdb
• 分子名称: FolM Alternative dihydrofolate reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: ssgcid, oxidoreductase, short chain dehydrogenase/reductase family, dihydrofolate reductase, nadp, brucella suis, structural genomics, seattle structural genomics center for infectious disease
• 由来する生物種: Brucella suis 92/29
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 122089.14

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2016-09-27, 公開日: 2016-10-12, 最終更新日: 2023-10-04)

主引用文献

Porter, I.,Neal, T.,Walker, Z.,Hayes, D.,Fowler, K.,Billups, N.,Rhoades, A.,Smith, C.,Smith, K.,Staker, B.L.,Dranow, D.M.,Mayclin, S.J.,Subramanian, S.,Edwards, T.E.,Myler, P.J.,Asojo, O.A.
Crystal structures of FolM alternative dihydrofolate reductase 1 from Brucella suis and Brucella canis.
Acta Crystallogr.,Sect.F, 78:31-38, 2022

PubMed Abstract: Members of the bacterial genus Brucella cause brucellosis, a zoonotic disease that affects both livestock and wildlife. Brucella are category B infectious agents that can be aerosolized for biological warfare. As part of the structural genomics studies at the Seattle Structural Genomics Center for Infectious Disease (SSGCID), FolM alternative dihydrofolate reductases 1 from Brucella suis and Brucella canis were produced and their structures are reported. The enzymes share ∼95% sequence identity but have less than 33% sequence identity to other homologues with known structure. The structures are prototypical NADPH-dependent short-chain reductases that share their highest tertiary-structural similarity with protozoan pteridine reductases, which are being investigated for rational therapeutic development.

PubMed: 34981773
DOI: 10.1107/S2053230X21013078

実験手法

X-RAY DIFFRACTION (1.7 Å)