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[[Image:2cro.gif|left|200px]]


{{Structure
==STRUCTURE OF PHAGE 434 CRO PROTEIN AT 2.35 ANGSTROMS RESOLUTION==
|PDB= 2cro |SIZE=350|CAPTION= <scene name='initialview01'>2cro</scene>, resolution 2.35&Aring;
<StructureSection load='2cro' size='340' side='right'caption='[[2cro]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[2cro]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phage_434 Phage 434]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CRO FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cro OCA], [https://pdbe.org/2cro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cro RCSB], [https://www.ebi.ac.uk/pdbsum/2cro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cro ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cro OCA], [http://www.ebi.ac.uk/pdbsum/2cro PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cro RCSB]</span>
[https://www.uniprot.org/uniprot/RCRO_BP434 RCRO_BP434] 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]]
'''STRUCTURE OF PHAGE 434 CRO PROTEIN AT 2.35 ANGSTROMS RESOLUTION'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cr/2cro_consurf.spt"</scriptWhenChecked>
==Overview==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
The crystal structure of phage 434 Cro protein has been determined and refined against 2.35 A data to an R-factor of 19.5%. The protein comprises five alpha-helices and shows the helix-turn-helix motif found in other repressor proteins.
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==About this Structure==
</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=2cro ConSurf].
2CRO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Phage_434 Phage 434]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CRO OCA].  
<div style="clear:both"></div>
 
__TOC__
==Reference==
</StructureSection>
Structure of phage 434 Cro protein at 2.35 A resolution., Mondragon A, Wolberger C, Harrison SC, J Mol Biol. 1989 Jan 5;205(1):179-88. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2647998 2647998]
[[Category: Large Structures]]
[[Category: Phage 434]]
[[Category: Phage 434]]
[[Category: Single protein]]
[[Category: Harrison SC]]
[[Category: Harrison, S C.]]
[[Category: Mondragon A]]
[[Category: Mondragon, A.]]
[[Category: Wolberger C]]
[[Category: Wolberger, C.]]
[[Category: gene regulating protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:25:34 2008''

Latest revision as of 09:18, 14 February 2024

STRUCTURE OF PHAGE 434 CRO PROTEIN AT 2.35 ANGSTROMS RESOLUTION

2cro, resolution 2.35Å

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