7q6d | pdb_00007q6d

E. coli FtsA 1-405 ATP 3 Ni

spinqualitylabelsall models 7q6d, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7q6d is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: ATP, MG, NI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FTSA_ECOLI Essential cell division protein that assists in the assembly of the Z ring (PubMed:11847116). May serve as the principal membrane anchor for the Z ring (PubMed:15752196). Also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN (PubMed:10027987, PubMed:24750258, PubMed:9282742, PubMed:9495771, PubMed:9603865, PubMed:9882666). Binds ATP (PubMed:11053380). Publication Abstract from PubMed During bacterial cell division, filaments of tubulin-like FtsZ form the Z-ring, which is the cytoplasmic scaffold for divisome assembly. In Escherichia coli, the actin homologue FtsA anchors the Z-ring to the membrane and recruits divisome components, including bitopic FtsN. FtsN regulates the periplasmic peptidoglycan synthase FtsWI. To characterize how FtsA regulates FtsN, we applied electron microscopy to show that E. coli FtsA forms antiparallel double filaments on lipid monolayers when bound to the cytoplasmic tail of FtsN. Using X-ray crystallography, we demonstrate that Vibrio maritimus FtsA crystallizes as an equivalent double filament. We identified an FtsA-FtsN interaction site in the IA-IC interdomain cleft of FtsA using X-ray crystallography and confirmed that FtsA forms double filaments in vivo by site-specific cysteine cross-linking. FtsA-FtsN double filaments reconstituted in or on liposomes prefer negative Gaussian curvature, like those of MreB, the actin-like protein of the elongasome. We propose that curved antiparallel FtsA double filaments together with treadmilling FtsZ filaments organize septal peptidoglycan synthesis in the division plane. Bacterial divisome protein FtsA forms curved antiparallel double filaments when binding to FtsN.,Nierhaus T, McLaughlin SH, Burmann F, Kureisaite-Ciziene D, Maslen SL, Skehel JM, Yu CWH, Freund SMV, Funke LFH, Chin JW, Lowe J Nat Microbiol. 2022 Oct;7(10):1686-1701. doi: 10.1038/s41564-022-01206-9. Epub , 2022 Sep 19. PMID:36123441 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cell division protein 3D structures

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