3ZYY

Reductive activator for corrinoid,iron-sulfur protein

Summary for 3ZYY

• Entry DOI: 10.2210/pdb3zyy/pdb
• Descriptor: IRON-SULFUR CLUSTER BINDING PROTEIN, FE2/S2 (INORGANIC) CLUSTER, PHOSPHATE ION, ... (7 entities in total)
• Functional Keywords: iron-sulfur-binding protein, ashka family, atpase
• Biological source: CARBOXYDOTHERMUS HYDROGENOFORMANS
• Total number of polymer chains: 2
• Total formula weight: 139088.74

Authors

Hennig, S.E.,Jeoung, J.-H.,Goetzl, S.,Dobbek, H. (deposition date: 2011-08-30, release date: 2012-04-04, Last modification date: 2024-05-08)

Primary citation

Hennig, S.E.,Jeoung, J.H.,Goetzl, S.,Dobbek, H.
Redox-Dependent Complex Formation by an ATP-Dependent Activator of the Corrinoid/Iron-Sulfur Protein.
Proc.Natl.Acad.Sci.USA, 109:5235-, 2012

PubMed Abstract: Movement, cell division, protein biosynthesis, electron transfer against an electrochemical gradient, and many more processes depend on energy conversions coupled to the hydrolysis of ATP. The reduction of metal sites with low reduction potentials (E(0') < -500 mV) is possible by connecting an energetical uphill electron transfer with the hydrolysis of ATP. The corrinoid-iron/sulfur protein (CoFeSP) operates within the reductive acetyl-CoA pathway by transferring a methyl group from methyltetrahydrofolate bound to a methyltransferase to the [Ni-Ni-Fe(4)S(4)] cluster of acetyl-CoA synthase. Methylation of CoFeSP only occurs in the low-potential Co(I) state, which can be sporadically oxidized to the inactive Co(II) state, making its reductive reactivation necessary. Here we show that an open-reading frame proximal to the structural genes of CoFeSP encodes an ATP-dependent reductive activator of CoFeSP. Our biochemical and structural analysis uncovers a unique type of reductive activator distinct from the electron-transferring ATPases found to reduce the MoFe-nitrogenase and 2-hydroxyacyl-CoA dehydratases. The CoFeSP activator contains an ASKHA domain (acetate and sugar kinases, Hsp70, and actin) harboring the ATP-binding site, which is also present in the activator of 2-hydroxyacyl-CoA dehydratases and a ferredoxin-like [2Fe-2S] cluster domain acting as electron donor. Complex formation between CoFeSP and its activator depends on the oxidation state of CoFeSP, which provides evidence for a unique strategy to achieve unidirectional electron transfer between two redox proteins.

PubMed: 22431597
DOI: 10.1073/PNAS.1117126109

Experimental method

X-RAY DIFFRACTION (2.2 Å)