4fmm
From Proteopedia
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{{STRUCTURE_4fmm| PDB=4fmm | SCENE= }} | {{STRUCTURE_4fmm| PDB=4fmm | SCENE= }} | ||
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===Dimeric Sec14 family homolog 3 from Saccharomyces cerevisiae presents some novel features of structure that lead to a surprising "dimer-monomer" state change induced by substrate binding=== | ===Dimeric Sec14 family homolog 3 from Saccharomyces cerevisiae presents some novel features of structure that lead to a surprising "dimer-monomer" state change induced by substrate binding=== | ||
| + | {{ABSTRACT_PUBMED_23519406}} | ||
| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/PDR16_YEAST PDR16_YEAST]] Has phosphatidylinositol transfer activity. Involved in the regulation of the phospholipid composition of plasma- and endomembranes. Altering plasma membrane composition may provide a possible mechanism for multidrug resistance. Involved in the regulation of sterol biosynthesis. Contributes to efficient phospholipase D1 activation in the regulation of phospholipid turnover.<ref>PMID:9890948</ref> <ref>PMID:10848624</ref> | ||
==About this Structure== | ==About this Structure== | ||
[[4fmm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FMM OCA]. | [[4fmm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FMM OCA]. | ||
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| + | ==Reference== | ||
| + | <ref group="xtra">PMID:023519406</ref><references group="xtra"/><references/> | ||
[[Category: Saccharomyces cerevisiae s288c]] | [[Category: Saccharomyces cerevisiae s288c]] | ||
[[Category: Gao, Y.]] | [[Category: Gao, Y.]] | ||
Revision as of 15:13, 19 June 2013
Contents |
Dimeric Sec14 family homolog 3 from Saccharomyces cerevisiae presents some novel features of structure that lead to a surprising "dimer-monomer" state change induced by substrate binding
Template:ABSTRACT PUBMED 23519406
Function
[PDR16_YEAST] Has phosphatidylinositol transfer activity. Involved in the regulation of the phospholipid composition of plasma- and endomembranes. Altering plasma membrane composition may provide a possible mechanism for multidrug resistance. Involved in the regulation of sterol biosynthesis. Contributes to efficient phospholipase D1 activation in the regulation of phospholipid turnover.[1] [2]
About this Structure
4fmm is a 2 chain structure with sequence from Saccharomyces cerevisiae s288c. Full crystallographic information is available from OCA.
Reference
- Yuan Y, Zhao W, Wang X, Gao Y, Niu L, Teng M. Dimeric Sfh3 has structural changes in its binding pocket that are associated with a dimer-monomer state transformation induced by substrate binding. Acta Crystallogr D Biol Crystallogr. 2013 Mar;69(Pt 3):313-23. doi:, 10.1107/S0907444912046161. Epub 2013 Feb 16. PMID:23519406 doi:10.1107/S0907444912046161
- ↑ van den Hazel HB, Pichler H, do Valle Matta MA, Leitner E, Goffeau A, Daum G. PDR16 and PDR17, two homologous genes of Saccharomyces cerevisiae, affect lipid biosynthesis and resistance to multiple drugs. J Biol Chem. 1999 Jan 22;274(4):1934-41. PMID:9890948
- ↑ Li X, Routt SM, Xie Z, Cui X, Fang M, Kearns MA, Bard M, Kirsch DR, Bankaitis VA. Identification of a novel family of nonclassic yeast phosphatidylinositol transfer proteins whose function modulates phospholipase D activity and Sec14p-independent cell growth. Mol Biol Cell. 2000 Jun;11(6):1989-2005. PMID:10848624
