Journal article 763 views
Functional and structural characterisation of a viral cytochromeb5
Emma L. Reid,
Karen D. Weynberg,
John Love,
Michail N. Isupov,
Jennifer A. Littlechild,
William H. Wilson,
Steven Kelly 
,
David C. Lamb,
Michael J. Allen
,
David C. Lamb,
Michael J. Allen
FEBS Letters, Volume: 587, Issue: 22, Pages: 3633 - 3639
Swansea University Author:
Steven Kelly
Full text not available from this repository: check for access using links below.
DOI (Published version): 10.1016/j.febslet.2013.09.035
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 cytoch...
| Published in: | FEBS Letters |
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| ISSN: | 0014-5793 |
| Published: |
Wiley
2013
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| Online Access: |
Check full text
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| URI: | https://cronfa.swan.ac.uk/Record/cronfa18159 |
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| 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. |
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| College: |
Faculty of Medicine, Health and Life Sciences |
| Issue: |
22 |
| Start Page: |
3633 |
| End Page: |
3639 |