4cro
From Proteopedia
(Difference between revisions)
| (9 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:4cro.gif|left|200px]] | ||
| - | + | ==PROTEIN-DNA CONFORMATIONAL CHANGES IN THE CRYSTAL STRUCTURE OF A LAMBDA CRO-OPERATOR COMPLEX== | |
| - | + | <StructureSection load='4cro' size='340' side='right'caption='[[4cro]], [[Resolution|resolution]] 3.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4cro]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CRO FirstGlance]. <br> | |
| - | + | </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=4cro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cro OCA], [https://pdbe.org/4cro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cro RCSB], [https://www.ebi.ac.uk/pdbsum/4cro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cro ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://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. | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cr/4cro_consurf.spt"</scriptWhenChecked> | |
| - | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |
| - | == | + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=4cro ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The structure of a complex of bacteriophage lambda Cro protein with a 17-base-pair operator has been determined at 3.9-A resolution. Isomorphous derivatives obtained by the synthesis of site-specific iodinated DNA oligomers were of critical importance in solving the structure. The crystal structure contains three independent Cro-operator complexes that have very similar, although not necessarily identical, conformations. In the complex, the protein dimer undergoes a large conformational change relative to the crystal structure of the free protein. One monomer rotates by about 40 degrees relative to the other, this being accomplished primarily by a twisting of the two beta-sheet strands that connect one monomer with the other. In the complex, the DNA is bent by about 40 degrees into the shape of a boomerang but maintains essentially Watson-Crick B-form. In contrast to other known protein-DNA complexes, the DNA is not stacked end-to-end. The structure confirms the general features of the model previously proposed for the interaction of Cro with DNA. | The structure of a complex of bacteriophage lambda Cro protein with a 17-base-pair operator has been determined at 3.9-A resolution. Isomorphous derivatives obtained by the synthesis of site-specific iodinated DNA oligomers were of critical importance in solving the structure. The crystal structure contains three independent Cro-operator complexes that have very similar, although not necessarily identical, conformations. In the complex, the protein dimer undergoes a large conformational change relative to the crystal structure of the free protein. One monomer rotates by about 40 degrees relative to the other, this being accomplished primarily by a twisting of the two beta-sheet strands that connect one monomer with the other. In the complex, the DNA is bent by about 40 degrees into the shape of a boomerang but maintains essentially Watson-Crick B-form. In contrast to other known protein-DNA complexes, the DNA is not stacked end-to-end. The structure confirms the general features of the model previously proposed for the interaction of Cro with DNA. | ||
| - | + | Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex.,Brennan RG, Roderick SL, Takeda Y, Matthews BW Proc Natl Acad Sci U S A. 1990 Oct;87(20):8165-9. PMID:2146682<ref>PMID:2146682</ref> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex., Brennan RG, Roderick SL, Takeda Y, Matthews BW | + | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4cro" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia virus Lambda]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Brennan RG]] | ||
| + | [[Category: Matthews BW]] | ||
| + | [[Category: Roderick SL]] | ||
| + | [[Category: Takeda Y]] | ||
Current revision
PROTEIN-DNA CONFORMATIONAL CHANGES IN THE CRYSTAL STRUCTURE OF A LAMBDA CRO-OPERATOR COMPLEX
| |||||||||||
