1f4n: Difference between revisions

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[[Image:1f4n.png|left|200px]]


{{STRUCTURE_1f4n|  PDB=1f4n  |  SCENE=  }}
==C2 CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.==
 
<StructureSection load='1f4n' size='340' side='right'caption='[[1f4n]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
===C2 CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1f4n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F4N FirstGlance]. <br>
{{ABSTRACT_PUBMED_11188696}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4n OCA], [https://pdbe.org/1f4n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f4n RCSB], [https://www.ebi.ac.uk/pdbsum/1f4n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f4n ProSAT]</span></td></tr>
[[1f4n]] is a 2 chain structure of [[Rop protein]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4N OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/ROP_ECOLX ROP_ECOLX] Regulates plasmid DNA replication by modulating the initiation of transcription of the primer RNA precursor. Processing of the precursor of the primer, RNAII, is inhibited by hydrogen bonding of RNAII to its complementary sequence in RNAI. ROP increases the affinity of RNAI for RNAII and thus decreases the rate of replication initiation events.
== 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/f4/1f4n_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=1f4n ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Rop protein|Rop protein]]
*[[Rop protein|Rop protein]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:011188696</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Bishop, B.]]
[[Category: Large Structures]]
[[Category: Brunger, A T.]]
[[Category: Bishop B]]
[[Category: Regan, L.]]
[[Category: Brunger AT]]
[[Category: Willis, M A.]]
[[Category: Regan L]]
[[Category: Dimer]]
[[Category: Willis MA]]
[[Category: Helix-turn-helix]]
[[Category: Homodimer]]
[[Category: Hydrophobic core packing]]
[[Category: Rop]]
[[Category: Thermodynamic stability]]
[[Category: Transcription]]
[[Category: Transcription regulation]]

Latest revision as of 07:10, 7 February 2024

C2 CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.

1f4n, resolution 1.90Å

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