1vqe: Difference between revisions

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[[Image:1vqe.jpg|left|200px]]


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==GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY MET 47 (V35I, I47M)==
The line below this paragraph, containing "STRUCTURE_1vqe", creates the "Structure Box" on the page.
<StructureSection load='1vqe' size='340' side='right'caption='[[1vqe]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1vqe]] 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=1VQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VQE FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#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=1vqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vqe OCA], [https://pdbe.org/1vqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vqe RCSB], [https://www.ebi.ac.uk/pdbsum/1vqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vqe ProSAT]</span></td></tr>
{{STRUCTURE_1vqe| PDB=1vqe |  SCENE= }}
</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/1vqe_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=1vqe ConSurf].
<div style="clear:both"></div>


'''GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY MET 47 (V35I, I47M)'''
==See Also==
 
*[[Single-stranded DNA-binding protein 3D structures|Single-stranded DNA-binding protein 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
 
==About this Structure==
1VQE is a [[Single protein]] structure of sequence from [http://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=1VQE OCA].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/8855252 8855252]
[[Category: Enterobacteria phage f1]]
[[Category: Enterobacteria phage f1]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Skinner, M M.]]
[[Category: Skinner MM]]
[[Category: Terwilliger, T C.]]
[[Category: Terwilliger TC]]
[[Category: Dna-binding protein]]
[[Category: Gene v]]
[[Category: Mutant]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 12:47:42 2008''

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 MET 47 (V35I, I47M)GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY MET 47 (V35I, I47M)

Structural highlights

1vqe 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 1.8Å
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

1vqe, resolution 1.80Å

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