CRAL_TRIO_NCRAL/TRIO, N-terminal domain
|SMART accession number:||SM01100|
|Interpro abstract (IPR011074):|
This all-alpha domain is often found N-terminal to CRAL-TRIO domains. Its function is unknown.
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- Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing CRAL_TRIO_N domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with CRAL_TRIO_N domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing CRAL_TRIO_N domain in the selected taxonomic class.
- Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Sha B, Phillips SE, Bankaitis VA, Luo M
- Crystal structure of the Saccharomyces cerevisiaephosphatidylinositol-transfer protein.
- Nature. 1998; 391: 506-10
- Display abstract
The yeast phosphatidylinositol-transfer protein (Sec14) catalyses exchangeof phosphatidylinositol and phosphatidylcholine between membrane bilayersin vitro. In vivo, Sec14 activity is essential for vesicle budding fromthe Golgi complex. Here we report a three-dimensional structure for Sec14at 2.5 A resolution. Sec14 consists of twelve alpha-helices, sixbeta-strands, eight 3(10)-helices and has two distinct domains. Thecarboxy-terminal domain forms a hydrophobic pocket which, in the crystalstructure, is occupied by two molecules of n-octyl-beta-D-glucopyranosideand represents the phospholipid-binding domain. This pocket is reinforcedby a string motif whose disruption in a sec14 temperature-sensitive mutantresults in destabilization of the phospholipid-binding domain. Finally, wehave identified an unusual surface helix that may play a critical role indriving Sec14-mediated phospholipid exchange. From this structure, wederive the first molecular clues into how a phosphatidylinositol-transferprotein functions.
- Structure (3D structures containing this domain)
3D Structures of CRAL_TRIO_N domains in PDB
PDB code Main view Title 1aua PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SEC14P FROM SACCHAROMYCES CEREVISIAE 1o6u The Crystal Structure of Human Supernatant Protein Factor 1oip The Molecular Basis of Vitamin E Retention: Structure of Human Alpha-Tocopherol Transfer Protein 1oiz The Molecular Basis of Vitamin E Retention: Structure of Human Alpha-Tocopherol Transfer Protein 1olm Supernatant Protein Factor in Complex with RRR-alpha-Tocopherylquinone: A Link between Oxidized Vitamin E and Cholesterol Biosynthesis 1r5l Crystal Structure of Human Alpha-Tocopherol Transfer Protein Bound to its Ligand 3b74 Crystal Structure of Yeast Sec14 Homolog Sfh1 in Complex with Phosphatidylethanolamine 3b7n Crystal Structure of Yeast Sec14 Homolog Sfh1 in Complex with Phosphatidylinositol 3b7q Crystal Structure of Yeast Sec14 Homolog Sfh1 in Complex with Phosphatidylcholine 3b7z Crystal Structure of Yeast Sec14 Homolog Sfh1 in Complex with Phosphatidylcholine or Phosphatidylinositol 3hx3 Crystal structure of CRALBP mutant R234W 3hy5 Crystal structure of CRALBP 3q8g Resurrection of a functional phosphatidylinositol transfer protein from a pseudo-Sec14 scaffold by directed evolution 3w67 Crystal structure of mouse alpha-tocopherol transfer protein in complex with alpha-tocopherol and phosphatidylinositol-(3,4)-bisphosphate 3w68 Crystal structure of mouse alpha-tocopherol transfer protein in complex with alpha-tocopherol and phosphatidylinositol-(4,5)-bisphosphate 4ciz Crystal structure of the complex of the Cellular Retinal Binding Protein with 9-cis-retinal 4cj6 Crystal structure of the complex of the Cellular Retinal Binding Protein Mutant R234W with 9-cis-retinal 4fmm 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 4j7p Crystal structure of Saccharomyces cerevisiae Sfh3 4j7q Crystal structure of Saccharomyces cerevisiae Sfh3 complexed with phosphatidylinositol
- Links (links to other resources describing this domain)
PFAM CRAL_TRIO_N INTERPRO IPR011074