X-ray diffraction analysis of gene V protein encoded by filamentous bacteriophage Ff

The gene V protein encoded by bacteriophage Ff is a single-stranded DNA binding protein and it plays an important role in the replication cycle of the phage. The crystal structure of the gene V protein was determined using multiwavelength anomalous diffraction on the selenomethionine-containing wild-type and isoleucine-47 $\to$ methionine mutant proteins with x-ray diffraction data phased to 2.5 A resolution. The structure of the wild-type protein was refined to an R factor of 19.1% using native data to 1.8 A resolution. The gene V protein monomer is largely composed of β-structures, including a distorted five stranded antiparallel β-barrel and two prominent extended β-hairpins. The two monomers are closely associated together to form a dimer. The DNA binding site of the protein was explored by the qualitative electrostatic potential calculations. The result from the preliminary x-ray diffraction analysis of co-crystals of gene V protein and oligonucleotides was also presented.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biophysics

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Zhang, Hong

Contributors dc:contributor

• Wang, Andrew H.J.

• Chemistry, Biochemistry
• Biophysics, General

Statement dc:rights

• Copyright 1994 Zhang, Hong

Language dc:language

eng

Identifier

AAI9512607
(UMI)AAI9512607

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/20593