5tsg

PilB from Geobacter metallireducens bound to ADP

spinqualitylabelsall models 5tsg, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5tsg is a 3 chain structure with sequence from Geobacter metallireducens GS-15. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.4011Å Ligands: ADP, FMT, MG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q39VU7_GEOMG Publication Abstract from PubMed Type IVa pili are protein filaments essential for virulence in many bacterial pathogens; they extend and retract from the surface of bacterial cells to pull the bacteria forward. The motor ATPase PilB powers pilus assembly. Here we report the structures of the core ATPase domains of Geobacter metallireducens PilB bound to ADP and the non-hydrolysable ATP analogue, AMP-PNP, at 3.4 and 2.3 A resolution, respectively. These structures reveal important differences in nucleotide binding between chains. Analysis of these differences reveals the sequential turnover of nucleotide, and the corresponding domain movements. Our data suggest a clockwise rotation of the central sub-pores of PilB, which through interactions with PilC, would support the assembly of a right-handed helical pilus. Our analysis also suggests a counterclockwise rotation of the C2 symmetric PilT that would enable right-handed pilus disassembly. The proposed model provides insight into how this family of ATPases can power pilus extension and retraction. The molecular mechanism of the type IVa pilus motors.,McCallum M, Tammam S, Khan A, Burrows LL, Howell PL Nat Commun. 2017 May 5;8:15091. doi: 10.1038/ncomms15091. PMID:28474682 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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