1gvp

<table><tr><td colspan='2'>[[1gvp]] is a 1 chain structure. 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>

</td></tr><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>

[[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).

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:9098886</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1gvp" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Gao, Y G]]

[[Category: Su, S]]

[[Category: Terwilliger, T C]]

[[Category: Wang, A H.J]]

[[Category: Zhang, H]]

[[Category: Dna-binding protein]]