7amy | pdb_00007amy

Nonameric cytoplasmic domain of FlhA from Vibrio parahaemolyticus

spinqualitylabelsall models 7amy, resolution 3.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7amy is a 9 chain structure with sequence from "oceanomonas_parahaemolytica"_(fujino_et_al._1951)_miyamoto_et_al._1961 "oceanomonas parahaemolytica" (fujino et al. 1951) miyamoto et al. 1961. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: flhA, C1S91_05000, C9I78_24000, CGI34_13080, D5E78_16030, E4P16_05430, F0L99_07770, WR32_16185 ("Oceanomonas parahaemolytica" (Fujino et al. 1951) Miyamoto et al. 1961) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0A0F5SXE4_VIBPH] Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin.[RuleBase:RU364093] Publication Abstract from PubMed Type three secretion is the mechanism of protein secretion found in bacterial flagella and injectisomes. At its centre is the export apparatus (EA), a complex of five membrane proteins through which secretion substrates pass the inner membrane. While the complex formed by four of the EA proteins has been well characterised structurally, little is known about the structure of the membrane domain of the largest subunit, FlhA in flagella, SctV in injectisomes. Furthermore, the biologically relevant nonameric assembly of FlhA/SctV has been infrequently observed and differences in conformation of the cytoplasmic portion of FlhA/SctV between open and closed states have been suggested to reflect secretion system specific differences. FlhA has been shown to bind to chaperone-substrate complexes in an open state, but in previous assembled ring structures, SctV is in a closed state. Here, we identify FlhA and SctV homologues that can be recombinantly produced in the oligomeric state and study them using cryo-electron microscopy. The structures of the cytoplasmic domains from both FlhA and SctV are in the open state and we observe a conserved interaction between a short stretch of residues at the N-terminus of the cytoplasmic domain, known as FlhAL/SctVL, with a groove on the adjacent protomer's cytoplasmic domain, which stabilises the nonameric ring assembly. Nonameric structures of the cytoplasmic domain of FlhA and SctV in the context of the full-length protein.,Kuhlen L, Johnson S, Cao J, Deme JC, Lea SM PLoS One. 2021 Jun 18;16(6):e0252800. doi: 10.1371/journal.pone.0252800., eCollection 2021. PMID:34143799 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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