3U90

apoferritin: complex with SDS

Summary for 3U90

• Entry DOI: 10.2210/pdb3u90/pdb
• Related: 3F32
• Descriptor: Ferritin light chain, DODECYL SULFATE, CADMIUM ION, ... (4 entities in total)
• Functional Keywords: four helix bundle, iron-binding protein, intracellular protein, metal binding protein
• Biological source: Equus caballus (horse)
• Total number of polymer chains: 1
• Total formula weight: 21262.94

Authors

Liu, R.,Bu, W.,Xi, J.,Mortazavi, S.R.,Cheung-Lau, J.C.,Dmochowski, I.J.,Loll, P.J. (deposition date: 2011-10-17, release date: 2012-04-25, Last modification date: 2023-09-13)

Primary citation

Liu, R.,Bu, W.,Xi, J.,Mortazavi, S.R.,Cheung-Lau, J.C.,Dmochowski, I.J.,Loll, P.J.
Beyond the detergent effect: a binding site for sodium dodecyl sulfate (SDS) in mammalian apoferritin.
Acta Crystallogr.,Sect.D, 68:497-504, 2012

PubMed Abstract: Although sodium dodecyl sulfate (SDS) is widely used as an anionic detergent, it can also exert specific pharmacological effects that are independent of the surfactant properties of the molecule. However, structural details of how proteins recognize SDS are scarce. Here, it is demonstrated that SDS binds specifically to a naturally occurring four-helix bundle protein: horse apoferritin. The X-ray crystal structure of the apoferritin-SDS complex was determined at a resolution of 1.9 Å and revealed that the SDS binds in an internal cavity that has previously been shown to recognize various general anesthetics. A dissociation constant of 24 ± 9 µM at 293 K was determined by isothermal titration calorimetry. SDS binds in this cavity by bending its alkyl tail into a horseshoe shape; the charged SDS head group lies in the opening of the cavity at the protein surface. This crystal structure provides insights into the protein-SDS interactions that give rise to binding and may prove useful in the design of novel SDS-like ligands for some proteins.

PubMed: 22525747
DOI: 10.1107/S0907444912002740

Experimental method

X-RAY DIFFRACTION (1.9 Å)