1orc: Difference between revisions
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[[Image:1orc.gif|left|200px]] | [[Image:1orc.gif|left|200px]] | ||
'''CRO REPRESSOR INSERTION MUTANT K56-[DGEVK]''' | {{Structure | ||
|PDB= 1orc |SIZE=350|CAPTION= <scene name='initialview01'>1orc</scene>, resolution 1.54Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= CRO MUTANT K56-[DGEVK] ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10710 Enterobacteria phage lambda]) | |||
}} | |||
'''CRO REPRESSOR INSERTION MUTANT K56-[DGEVK]''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ORC is a [ | 1ORC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORC OCA]. | ||
==Reference== | ==Reference== | ||
High-resolution structure of an engineered Cro monomer shows changes in conformation relative to the native dimer., Albright RA, Mossing MC, Matthews BW, Biochemistry. 1996 Jan 23;35(3):735-42. PMID:[http:// | High-resolution structure of an engineered Cro monomer shows changes in conformation relative to the native dimer., Albright RA, Mossing MC, Matthews BW, Biochemistry. 1996 Jan 23;35(3):735-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8547253 8547253] | ||
[[Category: Enterobacteria phage lambda]] | [[Category: Enterobacteria phage lambda]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: gene regulating protein]] | [[Category: gene regulating protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:14:33 2008'' | ||
Revision as of 11:14, 20 March 2008
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| 1orc, resolution 1.54Å | |||||||||||||
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| Gene: | CRO MUTANT K56-[DGEVK] (Enterobacteria phage lambda) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRO REPRESSOR INSERTION MUTANT K56-[DGEVK]
Overview
A rationally designed, genetically engineered, monomeric form of the Cro protein from bacteriophage lambda has been crystallized and its structure determined by isomorphous replacement and refined to a resolution of 1.54 A. The structure confirms the rationale of the design but, at the same time, reveals 1-2 A shifts throughout the monomer structure relative to the previously determined structure of the dimeric wild-type protein. These changes include a 1.6 A main-chain shift in part of the beta-sheet region of the molecule relative to the alpha-helical region and a 1.1 A shift of a buried phenylalanine within the core as well as a correlated 2.2 A shift in a solvent-exposed beta-hairpin. The conformational adjustments appear to reflect an inherent flexibility of the protein that is associated with its DNA-binding function.
About this Structure
1ORC is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.
Reference
High-resolution structure of an engineered Cro monomer shows changes in conformation relative to the native dimer., Albright RA, Mossing MC, Matthews BW, Biochemistry. 1996 Jan 23;35(3):735-42. PMID:8547253
Page seeded by OCA on Thu Mar 20 13:14:33 2008
