2cc7: Difference between revisions

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==COMPLEXES OF DODECIN WITH FLAVIN AND FLAVIN-LIKE LIGANDS==
 
==Complexes of Dodecin with Flavin and Flavin-like Ligands==
<StructureSection load='2cc7' size='340' side='right' caption='[[2cc7]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='2cc7' size='340' side='right' caption='[[2cc7]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LUM:LUMICHROME'>LUM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LUM:LUMICHROME'>LUM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mog|1mog]], [[2cc6|2cc6]], [[2cc8|2cc8]], [[2cc9|2cc9]], [[2ccb|2ccb]], [[2ccc|2ccc]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mog|1mog]], [[2cc6|2cc6]], [[2cc8|2cc8]], [[2cc9|2cc9]], [[2ccb|2ccb]], [[2ccc|2ccc]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cc7 OCA], [http://pdbe.org/2cc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cc7 RCSB], [http://www.ebi.ac.uk/pdbsum/2cc7 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cc7 OCA], [http://pdbe.org/2cc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cc7 RCSB], [http://www.ebi.ac.uk/pdbsum/2cc7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cc7 ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cc/2cc7_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cc/2cc7_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>

Revision as of 11:35, 23 May 2018

Complexes of Dodecin with Flavin and Flavin-like LigandsComplexes of Dodecin with Flavin and Flavin-like Ligands

Structural highlights

2cc7 is a 1 chain structure with sequence from Hals3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Dodecin is a small dodecameric flavoprotein from Halobacterium salinarum that contains two flavins stacked between two tryptophan residues to form an aromatic tetrade. The functional properties of heterologously expressed dodecin were investigated by fluorescence spectroscopy, which allowed the determination of dissociation constants for a number of protein-ligand complexes. The values obtained were in the nanomolar to micromolar range and correlate positively with the ligand size. These data were supplemented by X-ray crystal structures of the apododecin and holocomplexes with lumichrome, lumiflavin, riboflavin and FMN at resolutions between 1.55 to 1.95 A to unravel a gating mechanism as the structural basis for the preferential binding of the small ligands lumichrome and lumiflavin. The detailed analysis of the dodecin manifold for preferential binding of lumichrome and lumiflavin provides insight on a subatom level into a protein's strategy to gain selectivity for low molecular mass compounds by steric restrictions rather than specific interactions. Investigations on the ligand composition of a wild-type dodecin crystal (1.32 A resolution) support conclusions of functional and structural investigations on heterologously expressed dodecin, and strongly suggest that lumichrome, a molecule associated with the flavin metabolism, is a ligand of dodecin in vivo. Studies on mutant protein and a Halorhodospira halophila homologue spread the idea of a lumichrome binding system as a possible "waste"-trapping device, widely distributed in prokaryotes.

Dodecins: a family of lumichrome binding proteins.,Grininger M, Zeth K, Oesterhelt D J Mol Biol. 2006 Mar 31;357(3):842-57. Epub 2006 Jan 18. PMID:16460756[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Grininger M, Zeth K, Oesterhelt D. Dodecins: a family of lumichrome binding proteins. J Mol Biol. 2006 Mar 31;357(3):842-57. Epub 2006 Jan 18. PMID:16460756 doi:10.1016/j.jmb.2005.12.072

2cc7, resolution 1.80Å

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