3TYI

Crystal Structure of Cytochrome c - p-Sulfonatocalix[4]arene Complexes

Summary for 3TYI

• Entry DOI: 10.2210/pdb3tyi/pdb
• Descriptor: Cytochrome c iso-1, PROTOPORPHYRIN IX CONTAINING FE, 25,26,27,28-tetrahydroxypentacyclo[19.3.1.1~3,7~.1~9,13~.1~15,19~]octacosa-1(25),3(28),4,6,9(27),10,12,15(26),16,18,21,23-dodecaene-5,11,17,23-tetrasulfonic acid, ... (4 entities in total)
• Functional Keywords: all alpha, electron carrier protein, mitochondrion, electron transport
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Mitochondrion intermembrane space: P00044
• Total number of polymer chains: 2
• Total formula weight: 27610.79

Authors

Mc Govern, R.E.,Fernandes, H.,Khan, A.R.,Crowley, P.B. (deposition date: 2011-09-26, release date: 2012-05-02, Last modification date: 2023-09-13)

Primary citation

McGovern, R.E.,Fernandes, H.,Khan, A.R.,Power, N.P.,Crowley, P.B.
Protein camouflage in cytochrome c-calixarene complexes.
Nat Chem, 4:527-533, 2012

PubMed Abstract: Small molecules that recognize protein surfaces are important tools for modifying protein interaction properties. Since the 1980s, several thousand studies concerning calixarenes and host-guest interactions have been published. Although there is growing interest in protein-calixarene interactions, only limited structural information has been available to date. We now report the crystal structure of a protein-calixarene complex. The water-soluble p-sulfonatocalix[4]arene is shown to bind the lysine-rich cytochrome c at three different sites. Binding curves obtained from NMR titrations reveal an interaction process that involves two or more binding sites. Together, the data indicate a dynamic complex in which the calixarene explores the surface of cytochrome c. In addition to providing valuable information on protein recognition, the data also indicate that the calixarene is a mediator of protein-protein interactions, with potential applications in generating assemblies and promoting crystallization.

PubMed: 22717436
DOI: 10.1038/nchem.1342

Experimental method

X-RAY DIFFRACTION (1.399 Å)