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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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References listed in PDB file
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Key reference
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Title
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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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Authors
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S.Su,
Y.G.Gao,
H.Zhang,
T.C.Terwilliger,
A.H.Wang.
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Ref.
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Protein Sci, 1997,
6,
771-780.
[DOI no: ]
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PubMed id
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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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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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