1ae3: Difference between revisions
New page: left|200px<br /><applet load="1ae3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ae3, resolution 2.0Å" /> '''MUTANT R82C OF GENE V... |
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[[Image:1ae3.jpg|left|200px]]<br /><applet load="1ae3" size=" | [[Image:1ae3.jpg|left|200px]]<br /><applet load="1ae3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ae3, resolution 2.0Å" /> | caption="1ae3, resolution 2.0Å" /> | ||
'''MUTANT R82C OF GENE V PROTEIN (SINGLE-STRANDED DNA BINDING PROTEIN)'''<br /> | '''MUTANT R82C OF GENE V PROTEIN (SINGLE-STRANDED DNA BINDING PROTEIN)'''<br /> | ||
==Overview== | ==Overview== | ||
The high-resolution crystal structure of the gene V protein (GVP) from the | 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. | ||
==About this Structure== | ==About this Structure== | ||
1AE3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | 1AE3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AE3 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Gao, Y | [[Category: Gao, Y G.]] | ||
[[Category: Su, S.]] | [[Category: Su, S.]] | ||
[[Category: Terwilliger, T | [[Category: Terwilliger, T C.]] | ||
[[Category: Wang, A | [[Category: Wang, A H.J.]] | ||
[[Category: Zhang, H.]] | [[Category: Zhang, H.]] | ||
[[Category: dna replication]] | [[Category: dna replication]] | ||
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[[Category: single-stranded dna binding protein]] | [[Category: single-stranded dna binding protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:29 2008'' | ||
Revision as of 12:43, 21 February 2008
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MUTANT R82C OF GENE V PROTEIN (SINGLE-STRANDED DNA BINDING PROTEIN)
OverviewOverview
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.
About this StructureAbout this Structure
1AE3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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., Su S, Gao YG, Zhang H, Terwilliger TC, Wang AH, Protein Sci. 1997 Apr;6(4):771-80. PMID:9098886
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