Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of a putative molybdenum-cofactor (Moco) biosynthesis protein C (MoaC) from Sulfolobus tokodaii (ST0472) was determined at 2.2 A resolution. The crystal belongs to the monoclinic space group C2, with unit-cell parameters a = 123.31, b = 78.58, c = 112.67 A, beta = 118.1 degrees . The structure was solved by molecular replacement using the structure of Escherichia coli MoaC as the probe model. The asymmetric unit is composed of a hexamer arranged as a trimer of dimers with noncrystallographic 32 symmetry. The structure of ST0472 is very similar to that of E. coli MoaC; however, in the ST0472 protein an additional loop formed by the insertion of seven residues participates in intermonomer interactions and the new structure also reveals the formation of an interdimer beta-sheet. These features may contribute to the stability of the oligomeric state. Structure of a putative molybdenum-cofactor biosynthesis protein C (MoaC) from Sulfolobus tokodaii (ST0472).,Yoshida H, Yamada M, Kuramitsu S, Kamitori S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jul 1;64(Pt, 7):589-92. Epub 2008 Jun 11. PMID:18607082[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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