1lrp: Difference between revisions
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<StructureSection load='1lrp' size='340' side='right'caption='[[1lrp]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='1lrp' size='340' side='right'caption='[[1lrp]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1lrp]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1lrp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LRP FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lrp OCA], [https://pdbe.org/1lrp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lrp RCSB], [https://www.ebi.ac.uk/pdbsum/1lrp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lrp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/RPC1_LAMBD RPC1_LAMBD]] Repressor protein CI allows phage lambda to reside inactively in the chromosome of its host bacterium. This lysogenic state is maintained by binding of regulatory protein CI to the OR and OL operators, preventing transcription of proteins necessary for lytic development. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</div> | </div> | ||
<div class="pdbe-citations 1lrp" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1lrp" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 08:55, 28 April 2021
COMPARISON OF THE STRUCTURES OF CRO AND LAMBDA REPRESSOR PROTEINS FROM BACTERIOPHAGE LAMBDACOMPARISON OF THE STRUCTURES OF CRO AND LAMBDA REPRESSOR PROTEINS FROM BACTERIOPHAGE LAMBDA
Structural highlights
Function[RPC1_LAMBD] Repressor protein CI allows phage lambda to reside inactively in the chromosome of its host bacterium. This lysogenic state is maintained by binding of regulatory protein CI to the OR and OL operators, preventing transcription of proteins necessary for lytic development. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe three-dimensional structures of cro repressor protein and of the amino-terminal domain of lambda repressor protein, both from bacteriophage lambda, are compared. The second and third alpha-helices, alpha 2 and alpha 3, are shown to have essentially identical conformations in the two proteins, confirming the significance of the amino acid sequence homology previously noted between these and other DNA binding proteins in the region corresponding to these helices. The correspondence between the two-helical units in cro and lambda repressor protein is better than the striking agreement noted previously between two-helical units in cro and catabolite gene-activator protein. Parts of the first alpha-helices of repressor and cro show a structural correspondence that suggests a revised sequence homology between the two proteins in their extreme amino-terminal regions. In particular, there is a short loop between the alpha 1 and alpha 2 helices of lambda repressor that is missing from cro. This structural difference may account for the observed differences found with different cros and repressors in the pattern of phosphates whose ethylation prevents the binding of these proteins to their specific recognition sites. Although the two proteins have strikingly similar alpha 2-alpha 3 helical units that are presumed to bind to DNA in an essentially similar manner, stereochemical restrictions prevent the alpha 2-alpha 3 units of the respective proteins aligning on the DNA in exactly the same way. Comparison of the structures of cro and lambda repressor proteins from bacteriophage lambda.,Ohlendorf DH, Anderson WF, Lewis M, Pabo CO, Matthews BW J Mol Biol. 1983 Sep 25;169(3):757-69. PMID:6226802[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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