5zfr

Crystal structure of PilB, an extension ATPase motor of Type IV pilus, from Geobacter sulfurreducens

spinqualitylabelsall models 5zfr, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zfr is a 3 chain structure with sequence from Geobacter sulfurreducens PCA. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.1Å Ligands: PO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q74D28_GEOSL Publication Abstract from PubMed Type IVa pili are bacterial appendages involved in diverse physiological processes, including electron transfer in Geobacter sulfurreducens. ATP hydrolysis coupled with conformational changes powers the extension (PilB) and retraction (PilT) motors in the pilus machinery. We report the unliganded crystal structures of the core ATPase domain of PilB and PilT-4 from G. sulfurreducens at 3.1 and 2.6 A resolution, respectively. PilB structure revealed three distinct conformations, that is, open, closed, and open' which were previously proposed to be mediated by ATP/ADP binding. PilT-4 subunits, on the other hand, were observed in the closed state conformation. We further report that both PilB and PilT-4 hexamers have two high-affinity ATP-binding sites. Comparative structural analysis and solution data presented here supports the "symmetric rotary model" for these ATPase motors. Our data further suggest that pores of these motors rotate either clockwise or counterclockwise to facilitate assembly or disassembly of right-handed or left-handed pilus. DATABASE: Structural data are available in the RCSB PDB database under the PDB ID 5ZFQ (PilT-4), 5ZFR (PilB). Structural insights into the mechanism of Type IVa pilus extension and retraction ATPase motors.,Solanki V, Kapoor S, Thakur KG FEBS J. 2018 Sep;285(18):3402-3421. doi: 10.1111/febs.14619. Epub 2018 Aug 18. PMID:30066435 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA