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A Mimivirus Enzyme that Participates in Viral Entry.

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.

SUBMITTER: Klose T

PROVIDER: S-EPMC4456301 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature

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A Mimivirus Enzyme that Participates in Viral Entry.

Klose Thomas T Herbst Dominik A DA Zhu Hanyu H Max Joann P JP Kenttämaa Hilkka I HI Rossmann Michael G MG

Structure (London, England : 1993) 20150514 6

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-choli ...[more]

PMID: 25982526

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