1vqh
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=1vqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vqh OCA], [http://www.ebi.ac.uk/pdbsum/1vqh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vqh RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VQH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1VQH 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=1VQH 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 00:27:20 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 ILE 47 REPLACED BY MET 47 (I47M)
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
1VQH 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 00:27:20 2008
