1EZV

STRUCTURE OF THE YEAST CYTOCHROME BC1 COMPLEX CO-CRYSTALLIZED WITH AN ANTIBODY FV-FRAGMENT

Summary for 1EZV

• Entry DOI: 10.2210/pdb1ezv/pdb
• Related: 1BCC 1BE3 1BGY 1QCR 2BCC 3BCC
• Descriptor: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I, HEAVY CHAIN (VH) OF FV-FRAGMENT, LIGHT CHAIN (VL) OF FV-FRAGMENT, ... (17 entities in total)
• Functional Keywords: cytochrome bc1 complex, complex iii, qcr, mitochondria, yeast, antibody fv-fragment, stigmatellin, coenzyme q6, matrix processing peptidases, ubiquinone, electron transfer, proton transfer, q-cycle, oxidoreductase-electron transport complex, oxidoreductase/electron transport
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Mitochondrion inner membrane: P07256 P22289
• Total number of polymer chains: 11
• Total formula weight: 247126.27

Authors

Hunte, C.,Koepke, J.,Lange, C.,Rossmanith, T.,Michel, H. (deposition date: 2000-05-12, release date: 2001-05-16, Last modification date: 2025-12-17)

Primary citation

Hunte, C.,Koepke, J.,Lange, C.,Rossmanith, T.,Michel, H.
Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment.
Structure Fold.Des., 8:669-684, 2000

PubMed Abstract: The cytochrome bc(1) complex is part of the energy conversion machinery of the respiratory and photosynthetic electron transfer chains. This integral membrane protein complex catalyzes electron transfer from ubiquinol to cytochrome c. It couples the electron transfer to the electrogenic translocation of protons across the membrane via a so-called Q cycle mechanism.

PubMed: 10873857
DOI: 10.1016/S0969-2126(00)00152-0

Experimental method

X-RAY DIFFRACTION (2.3 Å)