1myk
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=1myk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myk OCA], [http://www.ebi.ac.uk/pdbsum/1myk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1myk RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MYK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1MYK 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=1MYK OCA]. |
==Reference== | ==Reference== | ||
Crystal structure, folding, and operator binding of the hyperstable Arc repressor mutant PL8., Schildbach JF, Milla ME, Jeffrey PD, Raumann BE, Sauer RT, Biochemistry. 1995 Jan 31;34(4):1405-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7827088 7827088] | Crystal structure, folding, and operator binding of the hyperstable Arc repressor mutant PL8., Schildbach JF, Milla ME, Jeffrey PD, Raumann BE, Sauer RT, Biochemistry. 1995 Jan 31;34(4):1405-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7827088 7827088] | ||
| + | [[Category: Enterobacteria phage p22]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Yersinia phage py54]] | ||
[[Category: Jeffrey, P D.]] | [[Category: Jeffrey, P D.]] | ||
[[Category: Milla, M E.]] | [[Category: Milla, M E.]] | ||
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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 22:22:54 2008'' |
Revision as of 19:22, 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 | ||||||
CRYSTAL STRUCTURE, FOLDING, AND OPERATOR BINDING OF THE HYPERSTABLE ARC REPRESSOR MUTANT PL8
Overview
Arc repressor is a small, dimeric DNA-binding protein that belongs to the ribbon-helix-helix family of transcription factors. Replacing Pro8 at the N-terminal end of the beta-sheet with leucine increases the stability of the mutant protein by 2.5 kcal/mol of dimer. However, this enhanced stability is achieved at the expense of significantly reduced DNA binding affinity. The structure of the PL8 mutant dimer has been determined to 2.4-A resolution by X-ray crystallography. The overall structure of the mutant is very similar to wild type, but Leu8 makes an additional interstrand hydrogen bond at each end of the beta-sheet of the mutant, increasing the total number of beta-sheet hydrogen bonds from six to eight. Comparison of the refolding and unfolding kinetics of the PL8 mutant and wild-type Arc shows that the enhanced stability of the mutant is accounted for by a decrease in the rate of protein unfolding, suggesting that the mutation acts to stabilize the native state and that the beta-sheet forms after the rate-limiting step in folding. The reduced operator affinity of the PL8 dimer appears to arise because the mutant cannot make the new interstrand hydrogen bonds and simultaneously make the wild-type set of contacts with operator DNA.
About this Structure
1MYK is a Single protein structure of sequence from Enterobacteria phage p22. Full crystallographic information is available from OCA.
Reference
Crystal structure, folding, and operator binding of the hyperstable Arc repressor mutant PL8., Schildbach JF, Milla ME, Jeffrey PD, Raumann BE, Sauer RT, Biochemistry. 1995 Jan 31;34(4):1405-12. PMID:7827088
Page seeded by OCA on Sun Mar 30 22:22:54 2008
