3l1m: Difference between revisions

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[[Image:3l1m.jpg|left|200px]]


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==Crystal Structure of a Ni-directed Dimer of Cytochrome cb562 with a Quinolate-Histidine Hybrid Coordination Motif==
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<StructureSection load='3l1m' size='340' side='right'caption='[[3l1m]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3l1m]] 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=3L1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L1M FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HQI:N-(8-HYDROXYQUINOLIN-5-YL)ACETAMIDE'>HQI</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
{{STRUCTURE_3l1m|  PDB=3l1m  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3l1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l1m OCA], [https://pdbe.org/3l1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l1m RCSB], [https://www.ebi.ac.uk/pdbsum/3l1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l1m ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function.
== 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/l1/3l1m_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3l1m ConSurf].
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein homodimerization is the simplest form of oligomerization that is frequently utilized for the construction of functional biological assemblies and the regulation of cellular pathways. Despite its simplicity, dimerization still poses an enormous challenge for protein engineering and chemical maniupulation, owing to the large molecular surfaces involved in this process. We report here the construction of a hybrid coordination motif-consisting of a natural (His) and a non-natural ligand (quinolate)-on the alpha-helical surface of cytochrome cb(562), which (a) simultaneously binds divalent metals with high affinity, (b) leads to a metal-induced increase in global protein stability, and importantly, (c) enables the formation of a discrete protein dimer, whose shape is dictated by the inner-sphere metal coordination geometry and closely approximates that of the DNA-binding domains of bZIP family transcription factors.


===Crystal Structure of a Ni-directed Dimer of Cytochrome cb562 with a Quinolate-Histidine Hybrid Coordination Motif===
Controlled Protein Dimerization through Hybrid Coordination Motifs.,Radford RJ, Nguyen PC, Ditri TB, Figueroa JS, Tezcan FA Inorg Chem. 2010 May 3;49(9):4362-9. PMID:20377257<ref>PMID:20377257</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3l1m" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_20377257}}, adds the Publication Abstract to the page
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 20377257 is the PubMed ID number.
*[[Cytochrome b5 3D structures|Cytochrome b5 3D structures]]
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== References ==
{{ABSTRACT_PUBMED_20377257}}
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
3L1M is a 1 chain structure 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=3L1M OCA].
 
==Reference==
<ref group="xtra">PMID:20377257</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Radford, R J.]]
[[Category: Large Structures]]
[[Category: Tezcan, F A.]]
[[Category: Radford RJ]]
[[Category: Electron transport]]
[[Category: Tezcan FA]]
[[Category: Four-helix bundle]]
[[Category: Interfacial nickel coordination]]
[[Category: Metal-binding]]
[[Category: Periplasm]]
[[Category: Transport]]
[[Category: V-shaped dimer]]
 
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