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PDBsum entry 1ae2
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DNA binding protein
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PDB id
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1ae2
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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DNA binding protein
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Title:
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Mutant l32r of gene v protein (single-stranded DNA binding protein)
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Structure:
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Gene v protein. Chain: a. Synonym: gvp. Engineered: yes. Mutation: yes
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Source:
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Escherichia coli. Organism_taxid: 562. Strain: k561. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: the l32r mutant was produced according to the published procedure, w.S. Sandberg, p.M. Schlunk, h.B. Zabin,t.C. Terwilliger, biochemistry 34, 11970-11978
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Biol. unit:
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Dimer (from PDB file)
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Resolution:
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2.00Å
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R-factor:
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0.223
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R-free:
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0.326
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Authors:
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S.Su,Y.-G.Gao,H.Zhang,T.C.Terwilliger,A.H.-J.Wang
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Key ref:
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S.Su
et al.
(1997).
Analyses of the stability and function of three surface mutants (R82C, K69H, and L32R) of the gene V protein from Ff phage by X-ray crystallography.
Protein Sci,
6,
771-780.
PubMed id:
DOI:
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Date:
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04-Mar-97
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Release date:
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04-Sep-97
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PROCHECK
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Headers
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References
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P69543
(G5P_BPF1) -
DNA-Binding protein G5P from Enterobacteria phage f1
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Seq:
Struc:
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87 a.a.
86 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Protein Sci
6:771-780
(1997)
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PubMed id:
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Analyses of the stability and function of three surface mutants (R82C, K69H, and L32R) of the gene V protein from Ff phage by X-ray crystallography.
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S.Su,
Y.G.Gao,
H.Zhang,
T.C.Terwilliger,
A.H.Wang.
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ABSTRACT
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The high-resolution crystal structure of the gene V protein (GVP) from the Ff
filamentous phages (M13, fl, fd) has been solved recently for the wild-type and
two surface mutant (Y41F and Y41H) proteins, leading to a plausible model for
the polymeric GVP-ssDNA complex (Guan Y, Zhang H, Wang AHJ, 1995, Protein Sci
4:187-197). The model of the complex shows extensive contacts between
neighboring dimer GVPs involving electrostatic interactions between the K69 from
one and the D79 and R82 from the next dimer. In addition, hydrophobic
interactions between the amino acids L32 and L44 from one and G23 from the next
dimer also contribute to the dimer-dimer interactions. Mutations at the L32,
K69, and R82 amino acid sites generally destabilize the protein and many of
these affect the function of the phage. We have studied the structural effects
of three mutant proteins involving those sites, i.e., L32R, K69H, and R82C, by
X-ray crystallographic analysis at 2.0 A resolution. In L32R GVP, the structural
perturbation is localized, whereas in K69H and R82C GVPs, some long-range
effects are also detected in addition to the local perturbation. We have
interpreted the protein stability and the functional properties associated with
those mutations in terms of the observed structural perturbations.
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Selected figure(s)
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Figure 5.
Fig. 5. uperposition of the wt-GVPand mutant GVP near themutatedaminoacids. A: Wt versus L3R. : Wt versus K69H. C: Wt
versus R82C. Thicklinesrepresentwt-GVPand thin linesrepresentthecorrespondingmutants.
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Figure 6.
Fig. 6. Continued.
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The above figures are
reprinted
by permission from the Protein Society:
Protein Sci
(1997,
6,
771-780)
copyright 1997.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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E.Scaltriti,
M.Tegoni,
C.Rivetti,
H.Launay,
J.Y.Masson,
A.H.Magadan,
D.Tremblay,
S.Moineau,
R.Ramoni,
J.Lichière,
V.Campanacci,
C.Cambillau,
and
M.Ortiz-Lombardía
(2009).
Structure and function of phage p2 ORF34(p2), a new type of single-stranded DNA binding protein.
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Mol Microbiol,
73,
1156-1170.
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PDB codes:
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M.Masso,
E.Mathe,
N.Parvez,
K.Hijazi,
and
I.I.Vaisman
(2009).
Modeling the functional consequences of single residue replacements in bacteriophage f1 gene V protein.
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Protein Eng Des Sel,
22,
665-671.
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H.Fan,
and
A.E.Mark
(2003).
Relative stability of protein structures determined by X-ray crystallography or NMR spectroscopy: a molecular dynamics simulation study.
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Proteins,
53,
111-120.
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C.K.Vaughan,
P.Harryson,
A.M.Buckle,
and
A.R.Fersht
(2002).
A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase.
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Acta Crystallogr D Biol Crystallogr,
58,
591-600.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
