3HCG

Structure of the C-terminal domain (MsrB) of Neisseria meningitidis PilB (reduced form)

Summary for 3HCG

• Entry DOI: 10.2210/pdb3hcg/pdb
• Related: 3HCH 3HCI 3HCJ
• Descriptor: Peptide methionine sulfoxide reductase msrA/msrB, PHOSPHATE ION (3 entities in total)
• Functional Keywords: pilb, methionine sulfoxide reductase b, reduced form, disulfide bond, electron transport, multifunctional enzyme, oxidoreductase, redox-active center, transport
• Biological source: Neisseria meningitidis serogroup A
• Total number of polymer chains: 4
• Total formula weight: 66252.76

Authors

Ranaivoson, F.M.,Kauffmann, B.,Favier, F. (deposition date: 2009-05-06, release date: 2009-10-13, Last modification date: 2024-10-16)

Primary citation

Ranaivoson, F.M.,Neiers, F.,Kauffmann, B.,Boschi-Muller, S.,Branlant, G.,Favier, F.
Methionine sulfoxide reductase B displays a high level of flexibility.
J.Mol.Biol., 394:83-93, 2009

PubMed Abstract: Methionine sulfoxide reductases (Msrs) are enzymes that catalyze the reduction of methionine sulfoxide back to methionine. In vivo, Msrs are essential in the protection of cells against oxidative damage to proteins and in the virulence of some bacteria. Two structurally unrelated classes of Msrs, named MsrA and MsrB, exist. MsrB are stereospecific to R epimer on the sulfur of sulfoxide. All MsrB share a common reductase step with the formation of a sulfenic acid intermediate. For the subclass of MsrB whose recycling process passes through the formation of an intradisulfide bond, the recycling reducer is thioredoxin. In the present study, X-ray structures of Neisseria meningitidis MsrB have been determined. The structures have a fold based on two beta-sheets, similar to the fold already described for other MsrB, with the recycling Cys63 located in a position favorable for disulfide bond formation with the catalytic Cys117. X-ray structures of Xanthomonas campestris MsrB have also been determined. In the C117S MsrB structure with a bound substrate, the recycling Cys31 is far from Ser117, with Trp65 being essential in the reductase step located in between. This positioning prevents the formation of the Cys31-Cys117 disulfide bond. In the oxidized structure, a drastic conformational reorganization of the two beta-sheets due to withdrawal of the Trp65 region from the active site, which remains compatible with an efficient thioredoxin-recycling process, is observed. The results highlight the remarkable structural malleability of the MsrB fold.

PubMed: 19733575
DOI: 10.1016/j.jmb.2009.08.073

Experimental method

X-RAY DIFFRACTION (1.82 Å)