Oxysterol-binding protein homolog
From Proteopedia
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| - | <StructureSection load='1zhy' size='340' side='right' caption=' | + | <StructureSection load='1zhy' size='340' side='right' caption='Yeast oxysterol-binding protein homolog 4 complex with cholesterol and Pb+2 ion (black) (PDB code [[1zhy]])' scene='80/801819/Cv/1'> |
== Function == | == Function == | ||
'''Oxysterol-binding protein homolog''' (Osh) mediate sterol transport from the ER to mitochondria. Sterols are synthesized in the ER and are present in membranes and affect the membrane fluidity and permeability<ref>PMID:29487131</ref>. '''Osh4''' or '''Kes1''' is involved in membrane and lipid trafficking through trans-Golgi network and endosomal systems<ref>PMID:22341443</ref>. | '''Oxysterol-binding protein homolog''' (Osh) mediate sterol transport from the ER to mitochondria. Sterols are synthesized in the ER and are present in membranes and affect the membrane fluidity and permeability<ref>PMID:29487131</ref>. '''Osh4''' or '''Kes1''' is involved in membrane and lipid trafficking through trans-Golgi network and endosomal systems<ref>PMID:22341443</ref>. | ||
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| - | == Disease == | ||
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| - | == Relevance == | ||
== Structural highlights == | == Structural highlights == | ||
| + | The structure of the complex between Osh4 and cholesterol shows the <scene name='80/801819/Cv/5'>cholesterol binding in a tunnel</scene> covered by a <scene name='80/801819/Cv/4'>lid formed by the protein N-terminal</scene> with the <scene name='80/801819/Cv/7'>ligand forming numerous interactions with Osh4</scene><ref>PMID:16136145</ref>. Water molecules are shown as red spheres. | ||
</StructureSection> | </StructureSection> | ||
Current revision
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3D structures of oxysterol-binding protein homolog
Updated on 29-November-2018
References
- ↑ Tian S, Ohta A, Horiuchi H, Fukuda R. Oxysterol-binding protein homologs mediate sterol transport from the endoplasmic reticulum to mitochondria in yeast. J Biol Chem. 2018 Apr 13;293(15):5636-5648. doi: 10.1074/jbc.RA117.000596. Epub, 2018 Feb 27. PMID:29487131 doi:http://dx.doi.org/10.1074/jbc.RA117.000596
- ↑ Mousley CJ, Yuan P, Gaur NA, Trettin KD, Nile AH, Deminoff SJ, Dewar BJ, Wolpert M, Macdonald JM, Herman PK, Hinnebusch AG, Bankaitis VA. A sterol-binding protein integrates endosomal lipid metabolism with TOR signaling and nitrogen sensing. Cell. 2012 Feb 17;148(4):702-15. doi: 10.1016/j.cell.2011.12.026. PMID:22341443 doi:http://dx.doi.org/10.1016/j.cell.2011.12.026
- ↑ Im YJ, Raychaudhuri S, Prinz WA, Hurley JH. Structural mechanism for sterol sensing and transport by OSBP-related proteins. Nature. 2005 Sep 1;437(7055):154-8. PMID:16136145 doi:http://dx.doi.org/10.1038/nature03923
