4b8n: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Cytochrome b5 of Ostreococcus tauri virus 2== | |||
=== | <StructureSection load='4b8n' size='340' side='right' caption='[[4b8n]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4b8n]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ostreococcus_tauri_virus_2 Ostreococcus tauri virus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B8N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B8N FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4b8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b8n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b8n RCSB], [http://www.ebi.ac.uk/pdbsum/4b8n PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 14alpha-demethylation. The crystal structure of the OtV-2 cytochrome b5 enzyme reveals a single domain, comprising four beta sheets, four alpha 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. | |||
Functional and structural characterisation of a viral cytochrome b5.,Reid EL, Weynberg KD, Love J, Isupov MN, Littlechild JA, Wilson WH, Kelly SL, Lamb DC, Allen MJ FEBS Lett. 2013 Nov 15;587(22):3633-9. doi: 10.1016/j.febslet.2013.09.035. Epub, 2013 Oct 4. PMID:24100138<ref>PMID:24100138</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ostreococcus tauri virus 2]] | [[Category: Ostreococcus tauri virus 2]] | ||
[[Category: Allen, M J | [[Category: Allen, M J]] | ||
[[Category: Isupov, M | [[Category: Isupov, M]] | ||
[[Category: Kelly, S L | [[Category: Kelly, S L]] | ||
[[Category: Lamb, D C | [[Category: Lamb, D C]] | ||
[[Category: Littlechild, J A | [[Category: Littlechild, J A]] | ||
[[Category: Love, J | [[Category: Love, J]] | ||
[[Category: Reid, E L | [[Category: Reid, E L]] | ||
[[Category: Weynberg, K D | [[Category: Weynberg, K D]] | ||
[[Category: Wilson, W H | [[Category: Wilson, W H]] | ||
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
[[Category: Viral cytochrome b5]] | [[Category: Viral cytochrome b5]] | ||
Revision as of 17:23, 4 January 2015
Cytochrome b5 of Ostreococcus tauri virus 2Cytochrome b5 of Ostreococcus tauri virus 2
Structural highlights
Publication Abstract from PubMedCytochrome 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 14alpha-demethylation. The crystal structure of the OtV-2 cytochrome b5 enzyme reveals a single domain, comprising four beta sheets, four alpha 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. Functional and structural characterisation of a viral cytochrome b5.,Reid EL, Weynberg KD, Love J, Isupov MN, Littlechild JA, Wilson WH, Kelly SL, Lamb DC, Allen MJ FEBS Lett. 2013 Nov 15;587(22):3633-9. doi: 10.1016/j.febslet.2013.09.035. Epub, 2013 Oct 4. PMID:24100138[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||