4pde

Crystal structure of FdhD in complex with GDP

spinqualitylabelsall models 4pde, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pde is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: GDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FDHD_ECOLI Required for formate dehydrogenase (FDH) activity (PubMed:3077634, PubMed:8522521, PubMed:22194618, PubMed:25649206). Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH. Specifically interacts with IscS and stimulates its cysteine desulfurase activity. Also binds the molybdenum cofactor (PubMed:22194618, PubMed:25649206). Required for activity of formate dehydrogenase N (FDH-N), formate dehydrogenase O (FDH-O) and formate dehydrogenase H (FDH-H) (PubMed:3077634, PubMed:8522521, PubMed:22194618). Publication Abstract from PubMed Formate dehydrogenases (FDHs) are of interest as they are natural catalysts that sequester atmospheric CO2, generating reduced carbon compounds with possible uses as fuel. FDHs activity in Escherichia coli strictly requires the sulphurtransferase EcFdhD, which likely transfers sulphur from IscS to the molybdenum cofactor (Mo-bisPGD) of FDHs. Here we show that EcFdhD binds Mo-bisPGD in vivo and has submicromolar affinity for GDP-used as a surrogate of the molybdenum cofactor's nucleotide moieties. The crystal structure of EcFdhD in complex with GDP shows two symmetrical binding sites located on the same face of the dimer. These binding sites are connected via a tunnel-like cavity to the opposite face of the dimer where two dynamic loops, each harbouring two functionally important cysteine residues, are present. On the basis of structure-guided mutagenesis, we propose a model for the sulphuration mechanism of Mo-bisPGD where the sulphur atom shuttles across the chaperone dimer. Sulphur shuttling across a chaperone during molybdenum cofactor maturation.,Arnoux P, Ruppelt C, Oudouhou F, Lavergne J, Siponen MI, Toci R, Mendel RR, Bittner F, Pignol D, Magalon A, Walburger A Nat Commun. 2015 Feb 4;6:6148. doi: 10.1038/ncomms7148. PMID:25649206 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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