1CRC

CYTOCHROME C AT LOW IONIC STRENGTH

Summary for 1CRC

• Entry DOI: 10.2210/pdb1crc/pdb
• Descriptor: CYTOCHROME C, HEME C (3 entities in total)
• Functional Keywords: ferric form, low ionic strength, mitochondrial electron transport
• Biological source: Equus caballus (horse)
• Cellular location: Mitochondrion matrix: P00004
• Total number of polymer chains: 2
• Total formula weight: 24740.28

Authors

Sanishvili, R.,Volz, K.W.,Westbrook, E.M.,Margoliash, E. (deposition date: 1995-03-22, release date: 1996-03-08, Last modification date: 2024-10-30)

Primary citation

Sanishvili, R.,Volz, K.W.,Westbrook, E.M.,Margoliash, E.
The low ionic strength crystal structure of horse cytochrome c at 2.1 A resolution and comparison with its high ionic strength counterpart.
Structure, 3:707-716, 1995

PubMed Abstract: Cytochrome c is an integral part of the mitochondrial respiratory chain. It is confined to the intermembrane space of mitochondria, and has the function of transferring electrons between its redox partners. Solution studies of cytochrome c indicate that the conformation of the molecule is sensitive to the ionic strength of the medium.

PubMed: 8591047
DOI: 10.1016/S0969-2126(01)00205-2

Experimental method

X-RAY DIFFRACTION (2.08 Å)