1e0j

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spinqualitylabelsall models PDB ID 1e0j Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 3.00Å
Ligands:	and
Gene:	GENE 4 (Bacteriophage T7)
Coordinates:	save as pdb, mmCIF, xml

GP4D HELICASE FROM PHAGE T7 ADPNP COMPLEX

Overview

We have determined the crystal structure of an active, hexameric fragment of the gene 4 helicase from bacteriophage T7. The structure reveals how subunit contacts stabilize the hexamer. Deviation from expected six-fold symmetry of the hexamer indicates that the structure is of an intermediate on the catalytic pathway. The structural consequences of the asymmetry suggest a "binding change" mechanism to explain how cooperative binding and hydrolysis of nucleotides are coupled to conformational changes in the ring that most likely accompany duplex unwinding. The structure of a complex with a nonhydrolyzable ATP analog provides additional evidence for this hypothesis, with only four of the six possible nucleotide binding sites being occupied in this conformation of the hexamer. This model suggests a mechanism for DNA translocation.

About this Structure

1E0J is a Single protein structure of sequence from Bacteriophage t7. Full crystallographic information is available from OCA.

Reference

Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides., Singleton MR, Sawaya MR, Ellenberger T, Wigley DB, Cell. 2000 Jun 9;101(6):589-600. PMID:10892646

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