2cjc
From Proteopedia
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|PDB= 2cjc |SIZE=350|CAPTION= <scene name='initialview01'>2cjc</scene>, resolution 1.85Å | |PDB= 2cjc |SIZE=350|CAPTION= <scene name='initialview01'>2cjc</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cjc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjc OCA], [http://www.ebi.ac.uk/pdbsum/2cjc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cjc RCSB]</span> | ||
}} | }} | ||
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[[Category: Seiler, F.]] | [[Category: Seiler, F.]] | ||
[[Category: Zeth, K.]] | [[Category: Zeth, K.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: FAD]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: SO4]] | ||
[[Category: flavoprotein]] | [[Category: flavoprotein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:22:17 2008'' |
Revision as of 23:22, 30 March 2008
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| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEXES OF DODECIN WITH FLAVIN AND FLAVIN-LIKE LIGANDS
Overview
Both extensive theoretical calculations and experimental data obtained during several decades leave little doubt that flavin adenine dinucleotide (FAD) exists in an open as well as in a closed conformation in aqueous solution. However, the knowledge about the intramolecularly stacked complex of FAD is constructed on indirect methods while direct structural evidence is lacking. Recently, dodecin was reported as an unspecific flavin binding protein which exhibits the unique binding mode of incorporating stacked dimers of flavins into a single binding pocket. Here, we show that FAD is not bound in this manner, but in monomers of intramolecularly stacked conformation. As resulting from the dodecin ligand binding characteristic, this FAD stacked conformation suggests to be directly sequestered from the aqueous solution and thus to be the first X-ray structural view on a FAD solution-stacked form. Moreover, in extraordinary FAD binding, dodecin serves as a model for studying bound monomeric (FAD) versus bound dimeric (e.g. riboflavin) flavin properties.
About this Structure
2CJC is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.
Reference
Dodecin sequesters FAD in closed conformation from the aqueous solution., Grininger M, Seiler F, Zeth K, Oesterhelt D, J Mol Biol. 2006 Dec 8;364(4):561-6. Epub 2006 Sep 5. PMID:17027852
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