3JQM

Binding of 5'-GTP to molybdenum cofactor biosynthesis protein MoaC from Thermus theromophilus HB8

Summary for 3JQM

• Entry DOI: 10.2210/pdb3jqm/pdb
• Related: 3JQJ 3JQK
• Descriptor: Molybdenum cofactor biosynthesis protein C, GUANOSINE-5'-TRIPHOSPHATE, CITRATE ANION, ... (7 entities in total)
• Functional Keywords: moac, molybdenum cofactor (moco), moco biosynthesis, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, biosynthetic protein, molybdenum cofactor biosynthesis
• Biological source: Thermus thermophilus
• Total number of polymer chains: 9
• Total formula weight: 161251.73

Authors

Kanaujia, S.P.,Jeyakanthan, J.,Nakagawa, N.,Sekar, K.,Shinkai, A.,Kuramitsu, S.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2009-09-07, release date: 2010-06-30, Last modification date: 2023-11-01)

Primary citation

Kanaujia, S.P.,Jeyakanthan, J.,Nakagawa, N.,Balasubramaniam, S.,Shinkai, A.,Kuramitsu, S.,Yokoyama, S.,Sekar, K.
Structures of apo and GTP-bound molybdenum cofactor biosynthesis protein MoaC from Thermus thermophilus HB8
Acta Crystallogr.,Sect.D, 66:821-833, 2010

PubMed Abstract: 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-adenosylmethionine-dependent 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.

PubMed: 20606263
DOI: 10.1107/S0907444910019074

Experimental method

X-RAY DIFFRACTION (2.5 Å)