1orc

<table><tr><td colspan='2'>[[1orc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ORC FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRO MUTANT K56-[DGEVK] ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10710 Bacteriophage lambda])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1orc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1orc OCA], [http://pdbe.org/1orc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1orc RCSB], [http://www.ebi.ac.uk/pdbsum/1orc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1orc ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/RCRO_LAMBD RCRO_LAMBD]] Cro represses genes normally expressed in early phage development and is necessary for the late stage of lytic growth. It does this by binding to the OL and OR operators regions normally used by the repressor protein for lysogenic maintenance.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:8547253</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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==See Also==

*[[Bacteriophage repressor 3D structures|Bacteriophage repressor 3D structures]]

== References ==

<references/>

[[Category: Bacteriophage lambda]]

[[Category: Albright, R A]]

[[Category: Matthews, B W]]

[[Category: Mossing, M C]]

[[Category: Gene regulating protein]]