1orc
From Proteopedia
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[[Image:1orc.gif|left|200px]] | [[Image:1orc.gif|left|200px]] | ||
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'''CRO REPRESSOR INSERTION MUTANT K56-[DGEVK]''' | '''CRO REPRESSOR INSERTION MUTANT K56-[DGEVK]''' | ||
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[[Category: Matthews, B W.]] | [[Category: Matthews, B W.]] | ||
[[Category: Mossing, M C.]] | [[Category: Mossing, M C.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:11:16 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:11, 3 May 2008
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 Sat May 3 04:11:16 2008
