2OHD

Crystal structure of hypothetical molybdenum cofactor biosynthesis protein C from Sulfolobus tokodaii

Summary for 2OHD

• Entry DOI: 10.2210/pdb2ohd/pdb
• Descriptor: Probable molybdenum cofactor biosynthesis protein C (2 entities in total)
• Functional Keywords: alpha + beta, biosynthetic protein
• Biological source: Sulfolobus tokodaii str. 7
• Total number of polymer chains: 6
• Total formula weight: 102912.74

Authors

Yoshida, H.,Yamada, M.,Kuramitsu, S.,Kamitori, S. (deposition date: 2007-01-10, release date: 2007-11-27, Last modification date: 2023-10-25)

Primary citation

Yoshida, H.,Yamada, M.,Kuramitsu, S.,Kamitori, S.
Structure of a putative molybdenum-cofactor biosynthesis protein C (MoaC) from Sulfolobus tokodaii (ST0472)
Acta Crystallogr.,Sect.F, 64:589-592, 2008

PubMed Abstract: The 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.

PubMed: 18607082
DOI: 10.1107/S174430910801590X

Experimental method

X-RAY DIFFRACTION (2.2 Å)