6OHL

Crystal structure of Fusobacterium nucleatum flavodoxin bound to flavin mononucleotide

6OHL の概要

• エントリーDOI: 10.2210/pdb6ohl/pdb
• 分子名称: Flavodoxin, FLAVIN MONONUCLEOTIDE, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: flavodoxin, reduction potential, flavin mononucleotide, electron transfer, electron transport
• 由来する生物種: Fusobacterium nucleatum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19873.40

構造登録者

Kolesnikov, M.,Murphy, M.E.P. (登録日: 2019-04-05, 公開日: 2019-06-05, 最終更新日: 2024-03-13)

主引用文献

Mothersole, R.G.,Macdonald, M.,Kolesnikov, M.,Murphy, M.E.P.,Wolthers, K.R.
Structural insight into the high reduction potentials observed for Fusobacterium nucleatum flavodoxin.
Protein Sci., 28:1460-1472, 2019

PubMed Abstract: Flavodoxins are small flavin mononucleotide (FMN)-containing proteins that mediate a variety of electron transfer processes. The primary sequence of flavodoxin from Fusobacterium nucleatum, a pathogenic oral bacterium, is marked with a number of distinct features including a glycine to lysine (K13) substitution in the highly conserved phosphate-binding loop (T/S-X-T-G-X-T), variation in the aromatic residues that sandwich the FMN cofactor, and a more even distribution of acidic and basic residues. The E (oxidized/semiquinone; -43 mV) and E (semiquinone/hydroquinone; -256 mV) are the highest recorded reduction potentials of known long-chain flavodoxins. These more electropositive values are a consequence of the apoprotein binding to the FMN hydroquinone anion with ~70-fold greater affinity compared to the oxidized form of the cofactor. Inspection of the FnFld crystal structure revealed the absence of a hydrogen bond between the protein and the oxidized FMN N5 atom, which likely accounts for the more electropositive E . The more electropositive E is likely attributed to only one negatively charged group positioned within 12 Å of the FMN N1. We show that natural substitutions of highly conserved residues partially account for these more electropositive reduction potentials.

PubMed: 31116469
DOI: 10.1002/pro.3661

実験手法

X-RAY DIFFRACTION (1.85 Å)