3CIX

X-RAY structure of the [FeFe]-hydrogenase maturase HydE from thermotoga maritima in complex with thiocyanate

Summary for 3CIX

• Entry DOI: 10.2210/pdb3cix/pdb
• Related: 3CIW
• Descriptor: FeFe-Hydrogenase maturase, GLYCEROL, THIOCYANATE ION, ... (11 entities in total)
• Functional Keywords: radical adomet protein, fefe-hydrogenase maturation, beta barrel, fe4s4 cluster, thiocyanate, fe2s2 cluster, adomet binding protein
• Biological source: Thermotoga maritima
• Total number of polymer chains: 1
• Total formula weight: 44326.85

Authors

Nicolet, Y.,Ruback, J.K.,Posewitz, M.C.,Amara, P.,Mathevon, C.,Atta, M.,Fontecave, M.,Fontecilla-Camps, J.C. (deposition date: 2008-03-12, release date: 2008-04-08, Last modification date: 2024-10-30)

Primary citation

Nicolet, Y.,Rubach, J.K.,Posewitz, M.C.,Amara, P.,Mathevon, C.,Atta, M.,Fontecave, M.,Fontecilla-Camps, J.C.
X-ray Structure of the [FeFe]-Hydrogenase Maturase HydE from Thermotoga maritima
J.Biol.Chem., 283:18861-18872, 2008

PubMed Abstract: Maturation of the [FeFe]-hydrogenase active site depends on at least the expression of three gene products called HydE, HydF, and HydG. We have solved the high resolution structure of recombinant, reconstituted S-adenosine-L-methionine-dependent HydE from Thermotoga maritima. Besides the conserved [Fe(4)S(4)] cluster involved in the radical-based reaction, this HydE was reported to have a second [Fe(4)S(4)] cluster coordinated by three Cys residues. However, in our crystals, depending on the reconstitution and soaking conditions, this second cluster is either a [Fe(2)S(2)] center, with water occupying the fourth ligand site or is absent. We have carried out site-directed mutagenesis studies on the related HydE from Clostridium acetobutylicum, along with in silico docking and crystal soaking experiments, to define the active site region and three anion-binding sites inside a large, positive cavity, one of which binds SCN(-) with high affinity. Although the overall triose-phosphate isomerase-barrel structure of HydE is very similar to that of biotin synthase, the residues that line the internal cavity are significantly different in the two enzymes.

PubMed: 18400755
DOI: 10.1074/jbc.M801161200

Experimental method

X-RAY DIFFRACTION (1.7 Å)