PDBsum entry 4z26

Oxidoreductase

PDB id: 4z26

Contents

Protein chains

(+ 2 more) 649 a.a.

Ligands

FAD ×8

Waters ×699

PDB id:

4z26

Name:

Oxidoreductase

Title:

Mimivirus r135 (residues 51-702)

Structure:

Putative gmc-type oxidoreductase r135. Chain: a, b, c, d, e, f, g, h. Fragment: unp residues 51-702. Engineered: yes

Source:

Acanthamoeba polyphaga mimivirus. Apmv. Organism_taxid: 212035. Gene: mimi_r135. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.92Å R-factor: 0.168 R-free: 0.214

Authors:

T.Klose,M.G.Rossmann

Key ref:

T.Klose et al. (2015). A Mimivirus Enzyme that Participates in Viral Entry. Structure, 23, 1058-1065. PubMed id: 25982526 DOI: 10.1016/j.str.2015.03.023

Date:

28-Mar-15 Release date: 13-May-15

Protein chains

Q5UPL2  (YR135_MIMIV) -  Putative GMC-type oxidoreductase R135 from Acanthamoeba polyphaga mimivirus

Seq: 702 a.a.

Struc: 649 a.a.

Enzyme reactions

• Enzyme class: E.C.1.-.-.-

DOI no: 10.1016/j.str.2015.03.023

Structure 23:1058-1065 (2015)

PubMed id: 25982526

A Mimivirus Enzyme that Participates in Viral Entry.

T.Klose, D.A.Herbst, H.Zhu, J.P.Max, H.I.Kenttämaa, M.G.Rossmann.

ABSTRACT

Mimivirus was initially identified as a bacterium because its dense, 125-nm-long fibers stained Gram-positively. These fibers probably play a role during the infection of some host cells. The normal hosts of Mimivirus are unknown, but in the laboratory Mimivirus is usually propagated in amoeba. The structure of R135, a major component of the fibrous outer layer of Mimivirus, has been determined to 2-Å resolution. The protein's structure is similar to that of members of the glucose-methanol-choline oxidoreductase family, which have an N-terminal FAD binding domain and a C-terminal substrate recognition domain. The closest homolog to R135 is an aryl-alcohol oxidase that participates in lignin biodegradation of plant cell walls. Thus R135 might participate in the degradation of their normal hosts, including some lignin-containing algae.