4m4w

Mechanistic implications for the bacterial primosome assembly of the structure of a helicase-helicase loader complex

spinqualitylabelsall models 4m4w, resolution 6.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4m4w is a 15 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168 and Geobacillus stearothermophilus. The December 2013 RCSB PDB Molecule of the Month feature on DNA Helicase by David Goodsell is 10.2210/rcsb_pdb/mom_2013_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 6.1Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed During the assembly of the bacterial loader-dependent primosome, helicase loader proteins bind to the hexameric helicase ring, deliver it onto the oriC DNA and then dissociate from the complex. Here, to provide a better understanding of this key process, we report the crystal structure of the ~570-kDa prepriming complex between the Bacillus subtilis loader protein and the Bacillus stearothermophilus helicase, as well as the helicase-binding domain of primase with a molar ratio of 6:6:3 at 7.5 A resolution. The overall architecture of the complex exhibits a three-layered ring conformation. Moreover, the structure combined with the proposed model suggests that the shift from the 'open-ring' to the 'open-spiral' and then the 'closed-spiral' state of the helicase ring due to the binding of single-stranded DNA may be the cause of the loader release. Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly.,Liu B, Eliason WK, Steitz TA Nat Commun. 2013;4:2495. doi: 10.1038/ncomms3495. PMID:24048025 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Helicase 3D structures RNA polymerase 3D structures

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