1vqd: Difference between revisions

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<StructureSection load='1vqd' size='340' side='right'caption='[[1vqd]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
<StructureSection load='1vqd' size='340' side='right'caption='[[1vqd]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1vqd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpf1 Bpf1]. 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>
<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='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>
</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>
</table>
== Function ==
== 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).  
[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]]
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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=1vqd 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=1vqd 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>
<div class="pdbe-citations 1vqd" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Single-stranded DNA-binding protein 3D structures|Single-stranded DNA-binding protein 3D structures]]
*[[Single-stranded DNA-binding protein 3D structures|Single-stranded DNA-binding protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bpf1]]
[[Category: Enterobacteria phage f1]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Skinner, M M]]
[[Category: Skinner MM]]
[[Category: Terwilliger, T C]]
[[Category: Terwilliger TC]]
[[Category: Dna binding protein]]
[[Category: Dna-binding protein]]
[[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 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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