5fv0 | pdb_00005fv0

The cytoplasmic domain of EssC

spinqualitylabelsall models 5fv0, resolution 2.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fv0 is a 2 chain structure with sequence from "bacillus_thermodenitrificans"_klaushofer_and_hollaus_1970 "bacillus thermodenitrificans" klaushofer and hollaus 1970. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PE, ATP, ONA Gene: eccC, essC, GTNG_0419 ("Bacillus thermodenitrificans" Klaushofer and Hollaus 1970) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ECCC_GEOTN] Part of the ESX specialized secretion system, which exports proteins from the cell including EsxA (ESAT-6) and EsxB (CFP-10) (By similarity). Might be the translocase subunit (PubMed:25865481). Probably only the first FtsK domain can hydrolyze ATP (PubMed:27130157).[UniProtKB:P9WNB1][UniProtKB:P9WNB3] Publication Abstract from PubMed The membrane-bound protein EssC is an integral component of the bacterial Type VII secretion system (T7SS), which is a determinant of virulence in important Gram-positive pathogens. The protein is predicted to consist of an intracellular repeat of forkhead-associated (FHA) domains at the N-terminus, two transmembrane helices and three P-loop-containing ATPase-type domains, D1-D3, forming the C-terminal intracellular segment. We present crystal structures of the N-terminal FHA domains (EssC-N) and a C-terminal fragment EssC-C from Geobacillus thermodenitrificans, encompassing two of the ATPase-type modules, D2 and D3. Module D2 binds ATP with high affinity whereas D3 does not. The EssC-N and EssC-C constructs are monomeric in solution, but the full-length recombinant protein, with a molecular mass of approximately 169 kDa, forms a multimer of approximately 1 MDa. The observation of protomer contacts in the crystal structure of EssC-C together with similarity to the DNA translocase FtsK, suggests a model for a hexameric EssC assembly. Such an observation potentially identifies the key, and to date elusive, component of pore formation required for secretion by this recently discovered secretion system. The juxtaposition of the FHA domains suggests potential for interacting with other components of the secretion system. The structural data were used to guide an analysis of which domains are required for the T7SS machine to function in pathogenic Staphylococcus aureus The extreme C-terminal ATPase domain appears to be essential for EssC activity as a key part of the T7SS, whereas D2 and FHA domains are required for the production of a stable and functional protein. EssC: domain structures inform on the elusive translocation channel in the Type VII secretion system.,Zoltner M, Ng WM, Money JJ, Fyfe PK, Kneuper H, Palmer T, Hunter WN Biochem J. 2016 Jul 1;473(13):1941-52. doi: 10.1042/BCJ20160257. Epub 2016 Apr, 29. PMID:27130157 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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