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

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Title: X-ray diffraction analysis of gene V protein encoded by filamentous bacteriophage Ff
Author(s): Zhang, Hong
Doctoral Committee Chair(s): Wang, Andrew H.-J
Department / Program: Biophysics and Computational Biology
Discipline: Biophysics
Degree Granting Institution: University of Illinois at Urbana-Champaign
Degree: Ph.D.
Genre: Dissertation
Subject(s): Chemistry, Biochemistry Biophysics, General
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.
Issue Date: 1994
Type: Text
Language: English
URI: http://hdl.handle.net/2142/20593
Rights Information: Copyright 1994 Zhang, Hong
Date Available in IDEALS: 2011-05-07
Identifier in Online Catalog: AAI9512607
OCLC Identifier: (UMI)AAI9512607
 

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