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4IAP

Crystal structure of PH domain of Osh3 from Saccharomyces cerevisiae

Summary for 4IAP
Entry DOI10.2210/pdb4iap/pdb
DescriptorOxysterol-binding protein homolog 3,Endolysin,Oxysterol-binding protein homolog 3, SULFATE ION (3 entities in total)
Functional Keywordsph domain, beta sandwitch, targeting, phosphoinositides, lipid binding protein- hydrorase complex, lipid binding protein/ hydrorase
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
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Cellular locationCytoplasm : P38713
Total number of polymer chains2
Total formula weight60260.57
Authors
Tong, J.,Im, Y.J. (deposition date: 2012-12-07, release date: 2013-07-31, Last modification date: 2023-11-08)
Primary citationTong, J.,Yang, H.,Yang, H.,Eom, S.H.,Im, Y.J.
Structure of osh3 reveals a conserved mode of phosphoinositide binding in oxysterol-binding proteins
Structure, 21:1203-1213, 2013
Cited by
PubMed Abstract: The oxysterol-binding protein (OSBP)-related proteins (ORPs) are conserved from yeast to humans, and implicated in the regulation of lipid homeostasis and in signaling pathways. Saccharomyces cerevisiae has seven ORPs (Osh1-Osh7) that share one unknown essential function. Here, we report the 1.5-2.3 Å structures of the PH domain and ORD (OSBP-related domain) of yeast Osh3 in apo-form or in complex with phosphatidylinositol 4-phosphate (PI[4]P). Osh3 recognizes PI(4)P by the highly conserved residues in the tunnel of ORD whereas it lacks sterol binding due to the narrow hydrophobic tunnel. Yeast complementation tests suggest that PI(4)P binding to PH and ORD is essential for function. This study suggests that the unifying feature in all ORP homologs is the binding of PI(4)P to ORD and sterol binding is additional to certain homologs. Structural modeling of full-length Osh3 is consistent with the concept that Osh3 is a lipid transfer protein or regulator in membrane contact sites.
PubMed: 23791945
DOI: 10.1016/j.str.2013.05.007
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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