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7K0I

Human serine palmitoyltransferase complex SPTLC1/SPLTC2/ssSPTa

Summary for 7K0I
Entry DOI10.2210/pdb7k0i/pdb
EMDB information22598
DescriptorSerine palmitoyltransferase 1, Serine palmitoyltransferase 2, Serine palmitoyltransferase small subunit A, ... (5 entities in total)
Functional Keywordssphingolipid, membrane protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains6
Total formula weight247794.12
Authors
Wang, Y.,Niu, Y.,Zhang, Z.,Zhao, H.,Myasnikov, A.,Kalathur, R.,Lee, C.H. (deposition date: 2020-09-04, release date: 2021-02-24, Last modification date: 2021-03-24)
Primary citationWang, Y.,Niu, Y.,Zhang, Z.,Gable, K.,Gupta, S.D.,Somashekarappa, N.,Han, G.,Zhao, H.,Myasnikov, A.G.,Kalathur, R.C.,Dunn, T.M.,Lee, C.H.
Structural insights into the regulation of human serine palmitoyltransferase complexes.
Nat.Struct.Mol.Biol., 28:240-248, 2021
Cited by
PubMed Abstract: Sphingolipids are essential lipids in eukaryotic membranes. In humans, the first and rate-limiting step of sphingolipid synthesis is catalyzed by the serine palmitoyltransferase holocomplex, which consists of catalytic components (SPTLC1 and SPTLC2) and regulatory components (ssSPTa and ORMDL3). However, the assembly, substrate processing and regulation of the complex are unclear. Here, we present 8 cryo-electron microscopy structures of the human serine palmitoyltransferase holocomplex in various functional states at resolutions of 2.6-3.4 Å. The structures reveal not only how catalytic components recognize the substrate, but also how regulatory components modulate the substrate-binding tunnel to control enzyme activity: ssSPTa engages SPTLC2 and shapes the tunnel to determine substrate specificity. ORMDL3 blocks the tunnel and competes with substrate binding through its amino terminus. These findings provide mechanistic insights into sphingolipid biogenesis governed by the serine palmitoyltransferase complex.
PubMed: 33558761
DOI: 10.1038/s41594-020-00551-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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