X-ray diffraction analysis of gene V protein encoded by filamentous bacteriophage Ff
Zhang, Hong
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https://hdl.handle.net/2142/20593
Description
Title
X-ray diffraction analysis of gene V protein encoded by filamentous bacteriophage Ff
Author(s)
Zhang, Hong
Issue Date
1994
Doctoral Committee Chair(s)
Wang, Andrew H.J.
Department of Study
Biophysics and Computational Biology
Discipline
Biophysics
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Biochemistry
Biophysics, General
Language
eng
Abstract
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 $\beta$-structures, including a distorted five stranded antiparallel $\beta$-barrel and two prominent extended $\beta$-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.
The crystal structures of four mutant gene V proteins were solved and refined to $\sim$2 A resolutions. Three of these mutants were apolar substitutions in the hydrophobic core of the protein. One mutant, Arg 82 $\to$ Cys, is at the protein surface and is involved in breaking up of a surface salt bridge. The effects of these substitutions on the stability of the protein were discussed.
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