4C1N

Corrinoid protein reactivation complex with activator

Summary for 4C1N

• Entry DOI: 10.2210/pdb4c1n/pdb
• Descriptor: CARBON MONOXIDE DEHYDROGENASE CORRINOID/IRON-SULFUR PROTEIN, GAMMA SUBUNIT, CO DEHYDROGENASE/ACETYL-COA SYNTHASE, IRON-SULFUR PROTEIN, IRON-SULFUR CLUSTER BINDING PROTEIN, ... (7 entities in total)
• Functional Keywords: oxidoreductase-metal binding protein complex, oxidoreductase/metal binding protein
• Biological source: CARBOXYDOTHERMUS HYDROGENOFORMANS; More
• Total number of polymer chains: 12
• Total formula weight: 555641.30

Authors

Hennig, S.E.,Goetzl, S.,Jeoung, J.H.,Bommer, M.,Lendzian, F.,Hildebrandt, P.,Dobbek, H. (deposition date: 2013-08-13, release date: 2014-08-13, Last modification date: 2024-05-08)

Primary citation

Hennig, S.E.,Goetzl, S.,Jeoung, J.H.,Bommer, M.,Lendzian, F.,Hildebrandt, P.,Dobbek, H.
ATP-Induced Electron Transfer by Redox-Selective Partner Recognition
Nat.Commun., 5:4626-, 2014

PubMed Abstract: Thermodynamically unfavourable electron transfers are enabled by coupling to an energy-supplying reaction. How the energy is transduced from the exergonic to the endergonic process is largely unknown. Here we provide the structural basis for an energy transduction process in the reductive activation of B12-dependent methyltransferases. The transfer of one electron from an activating enzyme to the cobalamin cofactor is energetically uphill and relies on coupling to an ATPase reaction. Our results demonstrate that the key to coupling is, besides the oxidation state-dependent complex formation, the conformational gating of the electron transfer. Complex formation induces a substitution of the ligand at the electron-accepting Co ion. Addition of ATP initiates electron transfer by provoking conformational changes that destabilize the complex. We show how remodelling of the electron-accepting Co(2+) promotes ATP-dependent electron transfer; an efficient strategy not seen in other electron-transferring ATPases.

PubMed: 25109607
DOI: 10.1038/NCOMMS5626

Experimental method

X-RAY DIFFRACTION (2.53 Å)