1vqa
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vqa OCA], [http://www.ebi.ac.uk/pdbsum/1vqa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vqa RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VQA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1VQA 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=1VQA OCA]. |
==Reference== | ==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] | 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: | + | [[Category: Enterobacteria phage f1]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Skinner, M M.]] | [[Category: Skinner, M M.]] | ||
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[[Category: mutant]] | [[Category: mutant]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:27:14 2008'' |
Revision as of 21:27, 30 March 2008
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| , resolution 1.8Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ALA 35 AND ILE 47 REPLACED BY LEU 47 (V35A, I47L)
Overview
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
1VQA is a Single protein structure of sequence from Enterobacteria phage f1. Full crystallographic information is available from 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:8855252
Page seeded by OCA on Mon Mar 31 00:27:14 2008
