{"doi":"10.1016/j.febslet.2013.09.035","title":"Functional and structural characterisation of a viral cytochrome <i>b</i>5","abstract":"<jats:p>Cytochrome <jats:italic>b</jats:italic>5 is a ubiquitous electron transport protein. The sequenced viral OtV‐2 genome, which infects <jats:italic>Ostreococcus tauri</jats:italic>, was predicted to encode a putative cytochrome <jats:italic>b</jats:italic>5 enzyme. Using purified OtV‐2 cytochrome <jats:italic>b</jats:italic>5 we confirm this protein has identical spectral properties to purified human cytochrome <jats:italic>b</jats:italic>5 and additionally that the viral enzyme can substitute for yeast cytochrome <jats:italic>b</jats:italic>5 in yeast cytochrome P450 51 mediated sterol 14α‐demethylation. The crystal structure of the OtV‐2 cytochrome <jats:italic>b</jats:italic>5 enzyme reveals a single domain, comprising four β sheets, four α 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 <jats:italic>b</jats:italic>5 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 <jats:italic>b</jats:italic>5 characterised. The lack of requirement for membrane attachment (in contrast to all other microsomal cytochrome <jats:italic>b</jats:italic>5s) 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 <jats:italic>b</jats:italic>5 metabolic activity at the extremes of cellular scale.</jats:p>","journal":"FEBS Letters","year":2013,"id":36980,"datarank":0.48360332917180243,"base_score":2.3978952727983707,"endowment":2.3978952727983707,"self_citation_contribution":0.3596842909197557,"citation_network_contribution":0.12391903825204677,"self_endowment_contribution":0.3596842909197557,"citer_contribution":0.12391903825204677,"corpus_percentile":null,"corpus_rank":null,"citation_count":10,"citer_count":7,"citers_with_citation_signal":7,"citers_with_endowment":7,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":48.75,"fair_percentile":44.94283201407212,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":186226,"name":"Karen D. 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