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Functional and structural characterisation of a viral cytochrome b5

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dc.contributor.author Reid, Emma L
dc.contributor.author Weynberg, Karen D
dc.contributor.author Isupov, Michail N
dc.contributor.author Littlechild, Jennifer A
dc.contributor.author Wilson, William H
dc.contributor.author Kelly, Steven L
dc.contributor.author Lamb, David C
dc.contributor.author Allen, Michael A
dc.contributor.author Love, John (J)
dc.date.accessioned 2013-12-06T05:46:56Z
dc.date.accessioned 2017-03-21T01:30:32Z
dc.date.accessioned 2018-11-01T03:17:30Z
dc.date.available 2013-12-06T05:46:56Z
dc.date.available 2017-03-21T01:30:32Z
dc.date.available 2018-11-01T03:17:30Z
dc.date.issued 2013-11-15
dc.identifier.citation Reid EL, Weynberg KD, Love J, Isupov MN, Littlechild JA, Wilson WH, Kelly SL, Lamb DC, Allen MJ (2013) Functional and structural characterisation of a viral cytochrome b5. FEBS Letters 587 (22): 3633-3639 en_US
dc.identifier.uri http://epubs.aims.gov.au/11068/5521
dc.description.abstract Cytochrome b5 is a ubiquitous electron transport protein. The sequenced viral OtV-2 genome, which infects Ostreococcus tauri, was predicted to encode a putative cytochrome b5 enzyme. Using purified OtV-2 cytochrome b5 we confirm this protein has identical spectral properties to purified human cytochrome b5 and additionally that the viral enzyme can substitute for yeast cytochrome b5 in yeast cytochrome P450 51 mediated sterol 14 alpha-demethylation. The crystal structure of the OtV-2 cytochrome b5 enzyme reveals a single domain, comprising four Beta sheets, four Beta helices and a haem moiety, which is similar to that found in larger eukaryotic cytochrome proteins. As a product of a horizontal gene transfer event involving a subdomain of the host fumarate reductase-like protein, OtV-2 cytochrome b5 appears to have diverged in function and is likely to have evolved an entirely new role for the virus during infection. Indeed, lacking a hydrophobic C-terminal anchor, OtV-2 encodes the first cytosolic cytochrome b5 characterised. The lack of requirement for membrane attachment (in contrast to all other microsomal cytochrome b5s) may be a reflection of the small size of the host cell, further emphasizes the unique nature of this virus gene product and draws attention to the potential importance of cytochrome b5 metabolic activity at the extremes of cellular scale. en_US
dc.description.sponsorship BBSRC en_US
dc.description.uri http://www.febsletters.org/article/S0014-5793(13)00730-8/abstract en_US
dc.language.iso en en_US
dc.publisher Elsevier en_US
dc.subject Virus en_US
dc.subject cytochrome b5 en_US
dc.subject crystallography en_US
dc.subject P450 catalysis en_US
dc.subject Ostreococcus tauri en_US
dc.title Functional and structural characterisation of a viral cytochrome b5 en_US
dc.type journal article en_US
dc.identifier.doi 10.1016/j.febslet.2013.09.035


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