1opc: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(19 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1opc.gif|left|200px]]<br />
<applet load="1opc" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1opc, resolution 1.95&Aring;" />
'''OMPR DNA-BINDING DOMAIN, ESCHERICHIA COLI'''<br />


==Overview==
==OMPR DNA-BINDING DOMAIN, ESCHERICHIA COLI==
BACKGROUND: The differential expression of the ompF and ompC genes is, regulated by two proteins that belong to the two component family of, signal transduction proteins: the histidine kinase, EnvZ, and the response, regulator, OmpR. OmpR belongs to a subfamily of at least 50 response, regulators with homologous C-terminal DNA-binding domains of approximately, 98 amino acids. Sequence homology with DNA-binding proteins of known, structure cannot be detected, and the lack of structural information has, prevented understanding of many of this familys functional properties., RESULTS: We have determined the crystal structure of the Escherichia coli, OmpR C-terminal domain at 1.95 A resolution. The structure consists of, three alpha helices packed against two antiparallel beta sheets. Two, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9016718 (full description)]]
<StructureSection load='1opc' size='340' side='right'caption='[[1opc]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1opc]] is a 1 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=1OPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OPC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</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=1opc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1opc OCA], [https://pdbe.org/1opc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1opc RCSB], [https://www.ebi.ac.uk/pdbsum/1opc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1opc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OMPR_ECOLI OMPR_ECOLI] The N-terminus of this protein is required for the transcriptional expression of both major outer membrane protein genes ompF and ompC; its C-terminal moiety mediates the multimerization of the OmpR protein. As a multimer, it turns on the expression of the ompC gene; as a monomer, it turns on the expression of the ompF gene.
== 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/op/1opc_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=1opc ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1OPC is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]]. Structure known Active Sites: ALP, RH and W1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OPC OCA]].
*[[Porin 3D structures|Porin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The DNA-binding domain of OmpR: crystal structures of a winged helix transcription factor., Martinez-Hackert E, Stock AM, Structure. 1997 Jan 15;5(1):109-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9016718 9016718]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Martinez-Hackert, E.]]
[[Category: Martinez-Hackert E]]
[[Category: Stock, A.M.]]
[[Category: Stock AM]]
[[Category: osmoregulation]]
[[Category: response regulator]]
[[Category: transcription regulation]]
[[Category: winged helix]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:48:42 2007''

Latest revision as of 08:02, 14 February 2024

OMPR DNA-BINDING DOMAIN, ESCHERICHIA COLI

1opc, resolution 1.95Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA