2K8D
Solution structure of a zinc-binding methionine sulfoxide reductase
Summary for 2K8D
| Entry DOI | 10.2210/pdb2k8d/pdb |
| NMR Information | BMRB: 15941 |
| Descriptor | Peptide methionine sulfoxide reductase msrB, ZINC ION (2 entities in total) |
| Functional Keywords | msrb, thermophilic, zn binding, reductase, metal-binding, oxidoreductase |
| Biological source | Methanothermobacter thermautotrophicus |
| Total number of polymer chains | 1 |
| Total formula weight | 17395.08 |
| Authors | Carella, M.,Ohlenschlager, O.,Gorlach, M. (deposition date: 2008-09-05, release date: 2008-12-16, Last modification date: 2024-05-01) |
| Primary citation | 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 Cited by 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: 21219456DOI: 10.1111/j.1365-2958.2010.07447.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
