1vqd: Difference between revisions

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New page: left|200px<br /><applet load="1vqd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vqd, resolution 1.82Å" /> '''GENE V PROTEIN MUTAN...
 
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[[Image:1vqd.jpg|left|200px]]<br /><applet load="1vqd" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1vqd, resolution 1.82&Aring;" />
'''GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY LEU 47 (V35I, I47L)'''<br />


==Overview==
==GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY LEU 47 (V35I, I47L)==
The problem of rationally engineering protein molecules can be simplified, where effects of mutations on protein function are additive. Crystal, structures of single and double mutants in the hydrophobic core of gene V, protein indicate that structural and functional effects of core mutations, are additive when the regions structurally influenced by the mutations do, not substantially overlap. These regions of influence can provide a simple, basis for identifying sets of mutations that will show additive effects.
<StructureSection load='1vqd' size='340' side='right'caption='[[1vqd]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1vqd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_f1 Enterobacteria phage f1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VQD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VQD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.82&#8491;</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=1vqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vqd OCA], [https://pdbe.org/1vqd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vqd RCSB], [https://www.ebi.ac.uk/pdbsum/1vqd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vqd ProSAT]</span></td></tr>
</table>
== Function ==
[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).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vq/1vqd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1vqd ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1VQD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_f1 Bacteriophage f1]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VQD OCA].
*[[Single-stranded DNA-binding protein 3D structures|Single-stranded DNA-binding protein 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Potential use of additivity of mutational effects in simplifying protein engineering., Skinner MM, Terwilliger TC, Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10753-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8855252 8855252]
[[Category: Enterobacteria phage f1]]
[[Category: Bacteriophage f1]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Skinner MM]]
[[Category: Skinner, M.M.]]
[[Category: Terwilliger TC]]
[[Category: Terwilliger, T.C.]]
[[Category: dna-binding protein]]
[[Category: gene v]]
[[Category: mutant]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:02:25 2007''

Latest revision as of 11:46, 14 February 2024

GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY LEU 47 (V35I, I47L)GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY LEU 47 (V35I, I47L)

Structural highlights

1vqd is a 1 chain structure with sequence from Enterobacteria phage f1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.82Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1vqd, resolution 1.82Å

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