2ccc: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ccc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CCC FirstGlance]. <br> | <table><tr><td colspan='2'>[[2ccc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CCC FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LFN:LUMIFLAVIN'>LFN</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LFN:LUMIFLAVIN'>LFN</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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mog|1mog]], [[2cc6|2cc6]], [[2cc7|2cc7]], [[2cc8|2cc8]], [[2cc9|2cc9]], [[2ccb|2ccb]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mog|1mog]], [[2cc6|2cc6]], [[2cc7|2cc7]], [[2cc8|2cc8]], [[2cc9|2cc9]], [[2ccb|2ccb]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ccc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ccc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ccc RCSB], [http://www.ebi.ac.uk/pdbsum/2ccc 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=2ccc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ccc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ccc RCSB], [http://www.ebi.ac.uk/pdbsum/2ccc PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Halobacterium salinarum]] | [[Category: Halobacterium salinarum]] | ||
[[Category: Grininger, M | [[Category: Grininger, M]] | ||
[[Category: Oesterhelt, D | [[Category: Oesterhelt, D]] | ||
[[Category: Zeth, K | [[Category: Zeth, K]] | ||
[[Category: Flavoprotein]] | [[Category: Flavoprotein]] | ||
Revision as of 21:05, 15 January 2015
COMPLEXES OF DODECIN WITH FLAVIN AND FLAVIN-LIKE LIGANDSCOMPLEXES OF DODECIN WITH FLAVIN AND FLAVIN-LIKE LIGANDS
Structural highlights
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 PubMedDodecin 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
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