1myl
From Proteopedia
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|LIGAND= | |LIGAND= | ||
|ACTIVITY= | |ACTIVITY= | ||
| - | |GENE= MUTATED ARC GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | |GENE= MUTATED ARC GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10754 Enterobacteria phage P22]) |
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1myl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myl OCA], [http://www.ebi.ac.uk/pdbsum/1myl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1myl RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MYL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1MYL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYL OCA]. |
==Reference== | ==Reference== | ||
Are buried salt bridges important for protein stability and conformational specificity?, Waldburger CD, Schildbach JF, Sauer RT, Nat Struct Biol. 1995 Feb;2(2):122-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7749916 7749916] | Are buried salt bridges important for protein stability and conformational specificity?, Waldburger CD, Schildbach JF, Sauer RT, Nat Struct Biol. 1995 Feb;2(2):122-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7749916 7749916] | ||
| + | [[Category: Enterobacteria phage p22]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Yersinia phage py54]] | ||
[[Category: Sauer, R T.]] | [[Category: Sauer, R T.]] | ||
[[Category: Schildbach, J F.]] | [[Category: Schildbach, J F.]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:22:57 2008'' |
Revision as of 19:23, 30 March 2008
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | MUTATED ARC GENE (Enterobacteria phage P22) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANCES PROTEIN STABILITY BUT DOES NOT REDUCE CONFORMATIONAL SPECIFICITY
Overview
The side chains of Arg 31, Glu 36 and Arg 40 in Arc repressor form a buried salt-bridge triad. The entire salt-bridge network can be replaced by hydrophobic residues in combinatorial randomization experiments resulting in active mutants that are significantly more stable than wild type. The crystal structure of one mutant reveals that the mutant side chains pack against each other in an otherwise wild-type fold. Thus, simple hydrophobic interactions provide more stabilizing energy than the buried salt bridge and confer comparable conformational specificity.
About this Structure
1MYL is a Single protein structure of sequence from Enterobacteria phage p22. Full crystallographic information is available from OCA.
Reference
Are buried salt bridges important for protein stability and conformational specificity?, Waldburger CD, Schildbach JF, Sauer RT, Nat Struct Biol. 1995 Feb;2(2):122-8. PMID:7749916
Page seeded by OCA on Sun Mar 30 22:22:57 2008
