2OSE

Crystal Structure of the Mimivirus Cyclophilin

Summary for 2OSE

• Entry DOI: 10.2210/pdb2ose/pdb
• Descriptor: Probable peptidyl-prolyl cis-trans isomerase, CHLORIDE ION (3 entities in total)
• Functional Keywords: mimivirus, cyclophilin, isomerase
• Biological source: Mimivirus
• Cellular location: Virion : Q5UP71
• Total number of polymer chains: 1
• Total formula weight: 26641.77

Authors

Eisenmesser, E.Z.,Thai, V.,Renesto, P.,Raoult, D. (deposition date: 2007-02-05, release date: 2007-12-18, Last modification date: 2023-08-30)

Primary citation

Thai, V.,Renesto, P.,Fowler, C.A.,Brown, D.J.,Davis, T.,Gu, W.,Pollock, D.D.,Kern, D.,Raoult, D.,Eisenmesser, E.Z.
Structural, biochemical, and in vivo characterization of the first virally encoded cyclophilin from the Mimivirus.
J.Mol.Biol., 378:71-86, 2008

PubMed Abstract: Although multiple viruses utilize host cell cyclophilins, including severe acute respiratory syndrome (SARS) and human immunodeficiency virus type-1(HIV-1), their role in infection is poorly understood. To help elucidate these roles, we have characterized the first virally encoded cyclophilin (mimicyp) derived from the largest virus discovered to date (the Mimivirus) that is also a causative agent of pneumonia in humans. Mimicyp adopts a typical cyclophilin-fold, yet it also forms trimers unlike any previously characterized homologue. Strikingly, immunofluorescence assays reveal that mimicyp localizes to the surface of the mature virion, as recently proposed for several viruses that recruit host cell cyclophilins such as SARS and HIV-1. Additionally mimicyp lacks peptidyl-prolyl isomerase activity in contrast to human cyclophilins. Thus, this study suggests that cyclophilins, whether recruited from host cells (i.e. HIV-1 and SARS) or virally encoded (i.e. Mimivirus), are localized on viral surfaces for at least a subset of viruses.

PubMed: 18342330
DOI: 10.1016/j.jmb.2007.08.051

Experimental method

X-RAY DIFFRACTION (2.04 Å)