6itc | pdb_00006itc

Structure of a substrate engaged SecA-SecY protein translocation machine

Loading... Status: waiting for Mol* initialization Structural highlights 6itc is a 7 chain structure with sequence from Aequorea victoria, Bacillus subtilis subsp. subtilis str. 168, Escherichia coli, Geobacillus thermodenitrificans NG80-2 and Lama glama. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.45Å Ligands: ADP, BEF, GYS, MG, PGV Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SECA_BACSU Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (By similarity).[HAMAP-Rule:MF_01382] Publication Abstract from PubMed The Sec61/SecY channel allows the translocation of many proteins across the eukaryotic endoplasmic reticulum membrane or the prokaryotic plasma membrane. In bacteria, most secretory proteins are transported post-translationally through the SecY channel by the SecA ATPase. How a polypeptide is moved through the SecA-SecY complex is poorly understood, as structural information is lacking. Here, we report an electron cryo-microscopy (cryo-EM) structure of a translocating SecA-SecY complex in a lipid environment. The translocating polypeptide chain can be traced through both SecA and SecY. In the captured transition state of ATP hydrolysis, SecA's two-helix finger is close to the polypeptide, while SecA's clamp interacts with the polypeptide in a sequence-independent manner by inducing a short beta-strand. Taking into account previous biochemical and biophysical data, our structure is consistent with a model in which the two-helix finger and clamp cooperate during the ATPase cycle to move a polypeptide through the channel. Structure of the substrate-engaged SecA-SecY protein translocation machine.,Ma C, Wu X, Sun D, Park E, Catipovic MA, Rapoport TA, Gao N, Li L Nat Commun. 2019 Jun 28;10(1):2872. doi: 10.1038/s41467-019-10918-2. PMID:31253804 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Green Fluorescent Protein 3D structures Preprotein translocase 3D structures SecA

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