1gvp

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(New page: 200px<br /><applet load="1gvp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gvp, resolution 1.6&Aring;" /> '''GENE V PROTEIN (SINGL...)
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[[Image:1gvp.gif|left|200px]]<br /><applet load="1gvp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gvp, resolution 1.6&Aring;" />
 
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'''GENE V PROTEIN (SINGLE-STRANDED DNA BINDING PROTEIN)'''<br />
 
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==Overview==
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==GENE V PROTEIN (SINGLE-STRANDED DNA BINDING PROTEIN)==
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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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<StructureSection load='1gvp' size='340' side='right'caption='[[1gvp]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1gvp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GVP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GVP FirstGlance]. <br>
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1GVP 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GVP OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gvp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gvp OCA], [https://pdbe.org/1gvp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gvp RCSB], [https://www.ebi.ac.uk/pdbsum/1gvp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gvp ProSAT]</span></td></tr>
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==Reference==
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</table>
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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., Su S, Gao YG, Zhang H, Terwilliger TC, Wang AH, Protein Sci. 1997 Apr;6(4):771-80. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9098886 9098886]
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== Function ==
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[https://www.uniprot.org/uniprot/G5P_BPF1 G5P_BPF1] Binds to DNA in a highly cooperative manner without pronounced sequence specificity. During synthesis of the single-stranded (progeny) viral DNA, prevents the conversion into the double-stranded replicative form. G5P is displaced by the capsid protein G8P during phage assembly on the inner bacterial membrane (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gv/1gvp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gvp ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Gao, Y.G.]]
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[[Category: Gao Y-G]]
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[[Category: Su, S.]]
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[[Category: Su S]]
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[[Category: Terwilliger, T.C.]]
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[[Category: Terwilliger TC]]
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[[Category: Wang, A.H.J.]]
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[[Category: Wang AH-J]]
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[[Category: Zhang, H.]]
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[[Category: Zhang H]]
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[[Category: dna replication]]
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[[Category: dna-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:18:33 2007''
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Current revision

GENE V PROTEIN (SINGLE-STRANDED DNA BINDING PROTEIN)

PDB ID 1gvp

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