Kanaujia, SP and Jeyakanthan, J and Nakagawa, N and Balasubramaniam, S and Shinkai, A and Kuramitsu, S and Yokoyama, S and Sekar, K (2010) Structures of apo and GTP-bound molybdenum cofactor biosynthesis protein MoaC from Thermus thermophilus HB8. In: Acta Crystallographica Section D, 66 (Part 7). pp. 821-833.Full text not available from this repository. (Request a copy)
The first step in the molybdenum cofactor (Moco) biosynthesis pathway involves the conversion of guanosine triphosphate (GTP) to precursor Z by two proteins (MoaA and MoaC). MoaA belongs to the S-adenosylmethioninedependent radical enzyme superfamily and is believed to generate protein and/or substrate radicals by reductive cleavage of S-adenosylmethionine using an Fe-S cluster. MoaC has been suggested to catalyze the release of pyrophosphate and the formation of the cyclic phosphate of precursor Z. However, structural evidence showing the binding of a substrate-like molecule to MoaC is not available. Here, apo and GTP-bound crystal structures of MoaC from Thermus thermophilus HB8 are reported. Furthermore, isothermal titration calorimetry experiments have been carried out in order to obtain thermodynamic parameters for the protein-ligand interactions. In addition, molecular-dynamics (MD) simulations have been carried out on the protein-ligand complex of known structure and on models of relevant complexes for which X-ray structures are not available. The biophysical, structural and MD results reveal the residues that are involved in substrate binding and help in speculating upon a possible mechanism.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to International Union of Crystallography.|
|Department/Centre:||Division of Information Sciences > BioInformatics Centre|
|Date Deposited:||15 Jul 2010 09:19|
|Last Modified:||15 Jul 2010 09:19|
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