1vqe: Difference between revisions

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==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)==
<StructureSection load='1vqe' size='340' side='right' caption='[[1vqe]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1vqe' size='340' side='right'caption='[[1vqe]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1vqe]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VQE FirstGlance]. <br>
<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>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vqe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1vqe RCSB], [http://www.ebi.ac.uk/pdbsum/1vqe PDBsum]</span></td></tr>
</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>
<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>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/VHED_BPF1 VHED_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).  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vq/1vqe_consurf.spt"</scriptWhenChecked>
     <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>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:8855252<ref>PMID:8855252</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Single-stranded DNA-binding protein|Single-stranded DNA-binding protein]]
*[[Single-stranded DNA-binding protein 3D structures|Single-stranded DNA-binding protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Enterobacteria phage f1]]
[[Category: Enterobacteria phage f1]]
[[Category: Skinner, M M]]
[[Category: Large Structures]]
[[Category: Terwilliger, T C]]
[[Category: Skinner MM]]
[[Category: Dna-binding protein]]
[[Category: Terwilliger TC]]
[[Category: Gene v]]
[[Category: Mutant]]

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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