3JQK
Crystal structure of the molybdenum cofactor biosynthesis protein C (TTHA1789) from Thermus Theromophilus HB8 (H32 FORM)
Summary for 3JQK
| Entry DOI | 10.2210/pdb3jqk/pdb |
| Related | 3JQJ 3JQM |
| Descriptor | Molybdenum cofactor biosynthesis protein C, PHOSPHATE ION, ACETATE ION, ... (4 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 | 1 |
| Total formula weight | 17159.80 |
| Authors | Kanaujia, S.P.,Jeyakanthan, J.,Nakagawa, N.,Sekar, K.,Baba, S.,Chen, L.,Liu, Z.-J.,Wang, B.-C.,Ebihara, A.,Kuramitsu, S.,Shinkai, A.,Shiro, Y.,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 Cited by 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: 20606263DOI: 10.1107/S0907444910019074 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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