5cro

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(New page: 200px<br /><applet load="5cro" size="450" color="white" frame="true" align="right" spinBox="true" caption="5cro, resolution 2.3&Aring;" /> '''REFINED STRUCTURE OF ...)
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[[Image:5cro.gif|left|200px]]<br /><applet load="5cro" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="5cro, resolution 2.3&Aring;" />
 
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'''REFINED STRUCTURE OF CRO REPRESSOR PROTEIN FROM BACTERIOPHAGE LAMBDA'''<br />
 
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==Overview==
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==REFINED STRUCTURE OF CRO REPRESSOR PROTEIN FROM BACTERIOPHAGE LAMBDA==
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The structure of the Cro repressor protein from phage lambda has been, refined to a crystallographic R-value of 19.3% at 2.3 A resolution. The re, fined model supports the structure as originally described in 1981 and, provides a basis for comparison with the Cro-operator complex described in, the accompanying paper. Changes in structure seen in different crystal, forms and modifications of Cro suggest that the individual subunits are, somewhat plastic in nature. In addition, the dimer of Cro suggests a high, degree of flexibility, which may be important in forming the Cro-DNA, complex.The structure of the Cro subunit as determined by NMR agrees, reasonably well with that in the crystals (root-mean-square discrepancy of, about 2 A for all atoms). There are, however, only a limited number of, intersubunit distance constraints and, presumably for this reason, the, different NMR models for the dimer vary substantially among themselves, (discrepancies of 1.3 to 5.5 A). Because of this variation it is not, possible to say whether the range of discrepancies between the X-ray and, NMR Cro dimers (2.9 to 7.5 A) represent a significant difference between, the X-ray and solution structures.It has previously been proposed that, substitutions of Tyr26 in Cro increase thermal stability by the "reverse, hydrophobic effect", i.e. by exposing 40% more hydrophobic surface to, solvent in the folded form than in the unfolded state. The refined, structure, however, suggests that Tyr26 is equally solvent exposed in the, folded and unfolded states. The most stabilizing substitution is, Tyr26--&gt;Asp and in this case it appears that interaction with an, alpha-helix dipole is at least partly responsible for the enhanced, stability.
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<StructureSection load='5cro' size='340' side='right'caption='[[5cro]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[5cro]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cro 1cro]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CRO FirstGlance]. <br>
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5CRO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1CRO. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5CRO OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5cro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cro OCA], [https://pdbe.org/5cro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cro RCSB], [https://www.ebi.ac.uk/pdbsum/5cro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cro ProSAT]</span></td></tr>
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Refined structure of Cro repressor protein from bacteriophage lambda suggests both flexibility and plasticity., Ohlendorf DH, Tronrud DE, Matthews BW, J Mol Biol. 1998 Jul 3;280(1):129-36. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9653036 9653036]
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</table>
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[[Category: Enterobacteria phage lambda]]
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== Function ==
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[[Category: Single protein]]
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[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.
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[[Category: Matthews, B.W.]]
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== Evolutionary Conservation ==
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[[Category: Ohlendorf, D.H.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Tronrud, D.E.]]
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Check<jmol>
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[[Category: PO4]]
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<jmolCheckbox>
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[[Category: gene regulating protein]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cr/5cro_consurf.spt"</scriptWhenChecked>
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[[Category: transcription regulation]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:27:20 2007''
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</jmolCheckbox>
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</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=5cro ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Escherichia virus Lambda]]
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[[Category: Large Structures]]
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[[Category: Matthews BW]]
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[[Category: Ohlendorf DH]]
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[[Category: Tronrud DE]]

Current revision

REFINED STRUCTURE OF CRO REPRESSOR PROTEIN FROM BACTERIOPHAGE LAMBDA

PDB ID 5cro

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