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Crystal structures, dynamics and functional implications of molybdenum-cofactor biosynthesis protein MogA from two thermophilic organisms

Kanaujia, Shankar Prasad and Jeyakanthan, Jeyaraman and Shinkai, Akeo and Kuramitsu, Seiki and Yokoyama, Shigeyuki and Sekar, Kanagaraj (2011) Crystal structures, dynamics and functional implications of molybdenum-cofactor biosynthesis protein MogA from two thermophilic organisms. In: Acta Crystallographica Section F, 67 (Part 1). pp. 2-16.

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Official URL: http://scripts.iucr.org/cgi-bin/paper?S17443091100...


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 angstrom resolution, space group P2(1)) and Aquifex aeolicus (AaMogA; 1.70 angstrom resolution, space group P2(1) and 1.90 angstrom 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.

Item Type: Journal Article
Publication: Acta Crystallographica Section F
Publisher: John Wiley and Sons
Additional Information: Copyright of this article belongs to John Wiley and Sons.
Keywords: MogA;molybdenum-cofactor biosynthesis proteins.
Department/Centre: Division of Information Sciences (Doesn't exist now) > BioInformatics Centre
Date Deposited: 06 May 2011 07:25
Last Modified: 06 May 2011 07:25
URI: http://eprints.iisc.ac.in/id/eprint/37401

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