2K8D

Solution structure of a zinc-binding methionine sulfoxide reductase

2K8D の概要

• エントリーDOI: 10.2210/pdb2k8d/pdb
• NMR情報: BMRB: 15941
• 分子名称: Peptide methionine sulfoxide reductase msrB, ZINC ION (2 entities in total)
• 機能のキーワード: msrb, thermophilic, zn binding, reductase, metal-binding, oxidoreductase
• 由来する生物種: Methanothermobacter thermautotrophicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17395.08

構造登録者

Carella, M.,Ohlenschlager, O.,Gorlach, M. (登録日: 2008-09-05, 公開日: 2008-12-16, 最終更新日: 2024-05-01)

主引用文献

Carella, M.,Becher, J.,Ohlenschlager, O.,Ramachandran, R.,Guhrs, K.H.,Wellenreuther, G.,Meyer-Klaucke, W.,Heinemann, S.H.,Gorlach, M.
Structure-function relationship in an archaebacterial methionine sulphoxide reductase B.
Mol.Microbiol., 79:342-358, 2011

PubMed Abstract: Oxidation of methionine to methionine sulphoxide (MetSO) may lead to loss of molecular integrity and function. This oxidation can be 'repaired' by methionine sulphoxide reductases (MSRs), which reduce MetSO back to methionine. Two structurally unrelated classes of MSRs, MSRA and MSRB, show stereoselectivity towards the S and the R enantiomer of the sulphoxide respectively. Interestingly, these enzymes were even maintained throughout evolution in anaerobic organisms. Here, the activity and the nuclear magnetic resonance (NMR) structure of MTH711, a zinc containing MSRB from the thermophilic, methanogenic archaebacterium Methanothermobacter thermoautotrophicus, are described. The structure appears more rigid as compared with similar MSRBs from aerobic and mesophilic organisms. No significant structural differences between the oxidized and the reduced MTH711 state can be deduced from our NMR data. A stable sulphenic acid is formed at the catalytic Cys residue upon oxidation of the enzyme with MetSO. The two non-zinc-binding cysteines outside the catalytic centre are not necessary for activity of MTH711 and are not situated close enough to the active-site cysteine to serve in regenerating the active centre via the formation of an intramolecular disulphide bond. These findings imply a reaction cycle that differs from that observed for other MSRBs.

PubMed: 21219456
DOI: 10.1111/j.1365-2958.2010.07447.x

実験手法

SOLUTION NMR