1h5w

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2.1A BACTERIOPHAGE PHI-29 CONNECTOR

Overview

The three-dimensional crystal structure of the bacteriophage phi29, connector has been solved and refined to 2.1A resolution. This 422 kDa, oligomeric protein connects the head of the phage to its tail and, translocates the DNA into the prohead during packaging. Each monomer has, an elongated shape and is composed of a central, mainly alpha-helical, domain that includes a three-helix bundle, a distal alpha/beta domain and, a proximal six-stranded SH3-like domain. The protomers assemble into a, 12-mer, propeller-like, super-structure with a 35 A wide central channel., The surface of the channel is mainly electronegative, but it includes two, lysine rings 20 A apart. On the external surface of the particle a, hydrophobic belt extends to the concave area below the SH3-like domain, which forms a crown that retains the particle in the head. The lipophilic, belt contacts the non-matching symmetry vertex of the capsid and forms a, bearing for the connector rotation. The structure suggests a translocation, mechanism in which the longitudinal displacement of the DNA along its axis, is coupled to connector spinning.

About this Structure

1H5W is a Single protein structure of sequence from Vibrio phage f237 with MPD as ligand. Full crystallographic information is available from OCA.

Reference

Detailed architecture of a DNA translocating machine: the high-resolution structure of the bacteriophage phi29 connector particle., Guasch A, Pous J, Ibarra B, Gomis-Ruth FX, Valpuesta JM, Sousa N, Carrascosa JL, Coll M, J Mol Biol. 2002 Jan 25;315(4):663-76. PMID:11812138

Page seeded by OCA on Tue Nov 20 16:25:49 2007