4yhc

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Crystal structure of the WD40 domain of SCAP from fission yeastCrystal structure of the WD40 domain of SCAP from fission yeast

Structural highlights

4yhc is a 2 chain structure with sequence from Schizosaccharomyces pombe 972h-. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.05Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SCAP_SCHPO Escort protein required for sre1 processing at low sterol as well as oxygen levels. May regulate export of the scp1/sre1 complex from the ER at low sterol or oxygen levels. 4-methyl sterols bound to scp1 may mask an ER-export signal in scp1 leading to retention of the complex in the ER. Release of 4-methyl sterols may trigger a conformational change in the SSC domain of scp1 unmasking the ER export signal leading to recruitment into COPII-coated vesicles, transport to the Golgi complex, proteolytic cleavage of sre1 in the Golgi, release of the transcription factor fragment of sre1 from the membrane, its import into the nucleus and up-regulation of genes required for ergosterol biosynthesis as well as anaerobic growth.[UniProtKB:P97260][1] [2]

References

  1. Hughes AL, Todd BL, Espenshade PJ. SREBP pathway responds to sterols and functions as an oxygen sensor in fission yeast. Cell. 2005 Mar 25;120(6):831-42. PMID:15797383 doi:http://dx.doi.org/10.1016/j.cell.2005.01.012
  2. Hughes AL, Lee CY, Bien CM, Espenshade PJ. 4-Methyl sterols regulate fission yeast SREBP-Scap under low oxygen and cell stress. J Biol Chem. 2007 Aug 17;282(33):24388-96. Epub 2007 Jun 26. PMID:17595166 doi:http://dx.doi.org/10.1074/jbc.M701326200

4yhc, resolution 2.05Å

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OCA