4B8N

Cytochrome b5 of Ostreococcus tauri virus 2

4B8N の概要

• エントリーDOI: 10.2210/pdb4b8n/pdb
• 分子名称: CYTOCHROME B5-HOST ORIGIN, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: electron transport, viral cytochrome b5
• 由来する生物種: OSTREOCOCCUS TAURI VIRUS 2
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 44486.71

構造登録者

Isupov, M.,Reid, E.L.,Weynberg, K.D.,Love, J.,Wilson, W.H.,Kelly, S.L.,Lamb, D.C.,Allen, M.J.,Littlechild, J.A. (登録日: 2012-08-28, 公開日: 2013-09-04, 最終更新日: 2023-12-20)

主引用文献

Reid, E.L.,Weynberg, K.D.,Love, J.,Isupov, M.N.,Littlechild, J.A.,Wilson, W.H.,Kelly, S.L.,Lamb, D.C.,Allen, M.J.
Functional and Structural Characterisation of a Viral Cytochrome B5.
FEBS Lett., 587:3633-, 2013

PubMed 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 14α-demethylation. The crystal structure of the OtV-2 cytochrome b5 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 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.

PubMed: 24100138
DOI: 10.1016/J.FEBSLET.2013.09.035

実験手法

X-RAY DIFFRACTION (1.95 Å)