PDBsum entry 2jzr

Electron transport

PDB id: 2jzr

Contents

Protein chain

144 a.a. *

* Residue conservation analysis

PDB id:

2jzr

Name:

Electron transport

Title:

Solution structure of the oxidized form (cys67-cys70) of the n- terminal domain of pilb from n. Meningitidis.

Structure:

Peptide methionine sulfoxide reductase msra/msrb. Chain: a. Fragment: thioredoxin domain. Synonym: thioredoxin. Engineered: yes

Source:

Neisseria meningitidis serogroup a. Gene: msrab, pilb. Expressed in: escherichia coli.

NMR struc:

20 models

Authors:

M.Quinternet,P.Tsan,F.Neiers,C.Beaufils,S.Boschi-Muller,M.Averlant- Petit,G.Branlant,M.Cung

Key ref:

M.Quinternet et al. (2008). Solution structure and dynamics of the reduced and oxidized forms of the N-terminal domain of PilB from Neisseria meningitidis. Biochemistry, 47, 8577-8589. PubMed id: 18651754

Date:

15-Jan-08 Release date: 29-Jul-08

Protein chain

Q9JWM8  (MSRAB_NEIMA) -  Peptide methionine sulfoxide reductase MsrA/MsrB from Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / Z2491)

Seq: 522 a.a.

Struc: 144 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class 2: E.C.1.8.4.11 - peptide-methionine (S)-S-oxide reductase.
• Reaction:
  1. L-methionyl-[protein] + [thioredoxin]-disulfide + H2O = L-methionyl- (S)-S-oxide-[protein] + [thioredoxin]-dithiol
  2. [thioredoxin]-disulfide + L-methionine + H2O = L-methionine (S)-S- oxide + [thioredoxin]-dithiol
• Enzyme class 3: E.C.1.8.4.12 - peptide-methionine (R)-S-oxide reductase.
• Reaction: L-methionyl-[protein] + [thioredoxin]-disulfide + H2O = L-methionyl-(R)- S-oxide-[protein] + [thioredoxin]-dithiol
• Cofactor: Se(2+); Zn(2+)

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Biochemistry 47:8577-8589 (2008)

PubMed id: 18651754

Solution structure and dynamics of the reduced and oxidized forms of the N-terminal domain of PilB from Neisseria meningitidis.

M.Quinternet, P.Tsan, F.Neiers, C.Beaufils, S.Boschi-Muller, M.C.Averlant-Petit, G.Branlant, M.T.Cung.

ABSTRACT

The secreted form of the PilB protein was proposed to be involved in pathogen survival fighting against the defensive host's oxidative burst. PilB protein is composed of three domains. The central and the C-terminal domains display methionine sulfoxide reductase A and B activities, respectively. The N-terminal domain, which possesses a CXXC motif, was recently shown to regenerate in vitro the reduced forms of the methionine sulfoxide reductase domains of PilB from their oxidized forms, as does the thioredoxin 1 from E. coli, via a disulfide bond exchange. The thioredoxin-like N-terminal domain belongs to the cytochrome maturation protein structural family, but it possesses a unique additional segment (99)FLHE (102) localized in a loop. This segment covers one edge of the active site in the crystal structure of the reduced form of the N-terminal domain of PilB. We have determined the solution structure and the dynamics of the N-terminal domain from Neisseria meningitidis, in its reduced and oxidized forms. The FLHE loop adopts, in both redox states, a well-defined conformation. Subtle conformational and dynamic changes upon oxidation are highlighted around the active site, as well as in the FLHE loop. The functional consequences of the cytochrome maturation protein topology and those of the presence of FLHE loop are discussed in relation to the enzymatic properties of the N-terminal domain.