3PJR

HELICASE SUBSTRATE COMPLEX

Summary for 3PJR

• Entry DOI: 10.2210/pdb3pjr/pdb
• Descriptor: 5'-D(*GP*CP*AP*GP*TP*GP*CP*TP*CP*GP*TP*TP*TP*TP*T)-3', 5'-D(*CP*GP*AP*GP*CP*AP*CP*TP*GP*C)-3', HELICASE PCRA, ... (4 entities in total)
• Functional Keywords: helicase, hydrolase-dna complex, hydrolase/dna
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 3
• Total formula weight: 90714.24

Authors

Velankar, S.S.,Soultanas, P.,Dillingham, M.S.,Subramanya, H.S.,Wigley, D.B. (deposition date: 1999-03-12, release date: 1999-04-08, Last modification date: 2023-12-27)

Primary citation

Velankar, S.S.,Soultanas, P.,Dillingham, M.S.,Subramanya, H.S.,Wigley, D.B.
Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
Cell(Cambridge,Mass.), 97:75-98, 1999

PubMed Abstract: We have determined two different structures of PcrA DNA helicase complexed with the same single strand tailed DNA duplex, providing snapshots of different steps on the catalytic pathway. One of the structures is of a complex with a nonhydrolyzable analog of ATP and is thus a "substrate" complex. The other structure contains a bound sulphate ion that sits in a position equivalent to that occupied by the phosphate ion produced after ATP hydrolysis, thereby mimicking a "product" complex. In both complexes, the protein is monomeric. Large and distinct conformational changes occur on binding DNA and the nucleotide cofactor. Taken together, these structures provide evidence against an "active rolling" model for helicase action but are instead consistent with an "inchworm" mechanism.

PubMed: 10199404
DOI: 10.1016/S0092-8674(00)80716-3

Experimental method

X-RAY DIFFRACTION (3.3 Å)