2e3s
From Proteopedia
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'''Crystal structure of CERT START domain co-crystallized with C24-ceramide (P21)''' | '''Crystal structure of CERT START domain co-crystallized with C24-ceramide (P21)''' | ||
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[[Category: Nishijima, M.]] | [[Category: Nishijima, M.]] | ||
[[Category: Wakatsuki, S.]] | [[Category: Wakatsuki, S.]] | ||
| - | [[Category: | + | [[Category: Ceramide transfer]] |
| - | [[Category: | + | [[Category: Cert]] |
| - | [[Category: | + | [[Category: Lipid transfer protein]] |
| - | [[Category: | + | [[Category: Lipid transport]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:52:14 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 22:52, 3 May 2008
Crystal structure of CERT START domain co-crystallized with C24-ceramide (P21)
Overview
In mammalian cells, ceramide is synthesized in the endoplasmic reticulum and transferred to the Golgi apparatus for conversion to sphingomyelin. Ceramide transport occurs in a nonvesicular manner and is mediated by CERT, a cytosolic 68-kDa protein with a C-terminal steroidogenic acute regulatory protein-related lipid transfer (START) domain. The CERT START domain efficiently transfers natural D-erythro-C16-ceramide, but not lipids with longer (C20) amide-acyl chains. The molecular mechanisms of ceramide specificity, both stereo-specific recognition and length limit, are not well understood. Here we report the crystal structures of the CERT START domain in its apo-form and in complex with ceramides having different acyl chain lengths. In these complex structures, one ceramide molecule is buried in a long amphiphilic cavity. At the far end of the cavity, the amide and hydroxyl groups of ceramide form a hydrogen bond network with specific amino acid residues that play key roles in stereo-specific ceramide recognition. At the head of the ceramide molecule, there is no extra space to accommodate additional bulky groups. The two aliphatic chains of ceramide are surrounded by the hydrophobic wall of the cavity, whose size and shape dictate the length limit for cognate ceramides. Furthermore, local high-crystallographic B-factors suggest that the alpha-3 and the Omega1 loop might work as a gate to incorporate the ceramide into the cavity. Thus, the structures demonstrate the structural basis for the mechanism by which CERT can distinguish ceramide from other lipid types yet still recognize multiple species of ceramides.
About this Structure
2E3S is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for specific lipid recognition by CERT responsible for nonvesicular trafficking of ceramide., Kudo N, Kumagai K, Tomishige N, Yamaji T, Wakatsuki S, Nishijima M, Hanada K, Kato R, Proc Natl Acad Sci U S A. 2008 Jan 15;105(2):488-93. Epub 2008 Jan 9. PMID:18184806 Page seeded by OCA on Sun May 4 01:52:14 2008
