3MCJ

Crystal structure of molybdenum cofactor biosynthesis (AQ_061) other form from aquifex aeolicus VF5

Summary for 3MCJ

• Entry DOI: 10.2210/pdb3mcj/pdb
• Related: 3MCI
• Descriptor: Molybdenum cofactor biosynthesis MOG, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: molybdopterin, mpt, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, lyase
• Biological source: Aquifex aeolicus
• Total number of polymer chains: 6
• Total formula weight: 115853.55

Authors

Jeyakanthan, J.,Kanaujia, S.P.,Sekar, K.,Agari, Y.,Ebihara, A.,Kuramitsu, S.,Shinkai, A.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2010-03-29, release date: 2011-01-19, Last modification date: 2023-11-01)

Primary citation

Kanaujia, S.P.,Jeyakanthan, J.,Shinkai, A.,Kuramitsu, S.,Yokoyama, S.,Sekar, K.
Crystal structures, dynamics and functional implications of molybdenum-cofactor biosynthesis protein MogA from two thermophilic organisms
Acta Crystallogr.,Sect.F, 67:2-16, 2011

PubMed Abstract: Molybdenum-cofactor (Moco) biosynthesis is an evolutionarily conserved pathway in almost all kingdoms of life, including humans. Two proteins, MogA and MoeA, catalyze the last step of this pathway in bacteria, whereas a single two-domain protein carries out catalysis in eukaryotes. Here, three crystal structures of the Moco-biosynthesis protein MogA from the two thermophilic organisms Thermus thermophilus (TtMogA; 1.64 Å resolution, space group P2(1)) and Aquifex aeolicus (AaMogA; 1.70 Å resolution, space group P2(1) and 1.90 Å resolution, space group P1) have been determined. The functional roles and the residues involved in oligomerization of the protein molecules have been identified based on a comparative analysis of these structures with those of homologous proteins. Furthermore, functional roles have been proposed for the N- and C-terminal residues. In addition, a possible protein-protein complex of MogA and MoeA has been proposed and the residues involved in protein-protein interactions are discussed. Several invariant water molecules and those present at the subunit interfaces have been identified and their possible structural and/or functional roles are described in brief. In addition, molecular-dynamics and docking studies with several small molecules (including the substrate and the product) have been carried out in order to estimate their binding affinities towards AaMogA and TtMogA. The results obtained are further compared with those obtained for homologous eukaryotic proteins.

PubMed: 21206014
DOI: 10.1107/S1744309110035037

Experimental method

X-RAY DIFFRACTION (1.9 Å)