4Z24
Mimivirus R135 (residues 51-702)
Summary for 4Z24
| Entry DOI | 10.2210/pdb4z24/pdb |
| Related | 4Z25 4Z26 |
| Descriptor | GMC-type oxidoreductase R135, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | gmc oxidoreductase, fad, fiber, oxidoreductase |
| Biological source | Acanthamoeba polyphaga mimivirus (APMV) |
| Total number of polymer chains | 2 |
| Total formula weight | 144281.96 |
| Authors | Klose, T.,Rossmann, M.G. (deposition date: 2015-03-28, release date: 2015-04-15, Last modification date: 2023-09-27) |
| Primary citation | Klose, T.,Herbst, D.A.,Zhu, H.,Max, J.P.,Kenttamaa, H.I.,Rossmann, M.G. A Mimivirus Enzyme that Participates in Viral Entry. Structure, 23:1058-1065, 2015 Cited by PubMed 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. PubMed: 25982526DOI: 10.1016/j.str.2015.03.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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