PDBsum entry 5dip

Oxidoreductase

PDB id: 5dip

Contents

Protein chains

112 a.a.

Ligands

GOL

Metals

_NA ×3

Waters ×210

PDB id:

5dip

Name:

Oxidoreductase

Title:

Crystal structure of lpg0406 in reduced form from legionella pneumophila

Structure:

Alkyl hydroperoxide reductase ahpd. Chain: a, b. Synonym: alkylhydroperoxidase. Engineered: yes

Source:

Legionella pneumophila. Organism_taxid: 446. Gene: lptwr_00386, lpymg_00422. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.10Å R-factor: 0.135 R-free: 0.158

Authors:

X.Chen,X.Gong,N.Zhang,H.Ge

Key ref:

X.Chen et al. (2015). Structure of lpg0406, a carboxymuconolactone decarboxylase family protein possibly involved in antioxidative response from Legionella pneumophila. Protein Sci, 24, 2070-2075. PubMed id: 26402328 DOI: 10.1002/pro.2811

Date:

01-Sep-15 Release date: 14-Oct-15

Protein chains

Q5ZYG6  (Q5ZYG6_LEGPH) -  Carboxymuconolactone decarboxylase-like domain-containing protein from Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)

Seq: 113 a.a.

Struc: 112 a.a.

Enzyme reactions

• Enzyme class: E.C.1.11.1.15 - Transferred entry: 1.11.1.24, 1.11.1.25, 1.11.1.26, 1.11.1.27, 1.11.1.28
• Pathway: Peroxiredoxin
• Reaction: 2 R'-SH + ROOH = R'-S-S-R' + H₂O + ROH

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

reference

DOI no: 10.1002/pro.2811

Protein Sci 24:2070-2075 (2015)

PubMed id: 26402328

Structure of lpg0406, a carboxymuconolactone decarboxylase family protein possibly involved in antioxidative response from Legionella pneumophila.

X.Chen, Y.Hu, B.Yang, X.Gong, N.Zhang, L.Niu, Y.Wu, H.Ge.

ABSTRACT

Lpg0406, a hypothetical protein from Legionella pneumophila, belongs to carboxymuconolactone decarboxylase (CMD) family. We determined the crystal structure of lpg0406 both in its apo and reduced form. The structures reveal that lpg0406 forms a hexamer and have disulfide exchange properties. The protein has an all-helical fold with a conserved thioredoxin-like active site CXXC motif and a proton relay system similar to that of alkylhydroperoxidase from Mycobacterium tuberculosis (MtAhpD), suggesting that lpg0406 might function as an enzyme with peroxidase activity and involved in antioxidant defense. A comparison of the size and the surface topology of the putative substrate-binding region between lpg0406 and MtAhpD indicates that the two enzymes accommodate the different substrate preferences. The structural findings will enhance understanding of the CMD family protein structure and its various functions.