2fb2
From Proteopedia
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'''Structure of the MoaA Arg17/266/268/Ala triple mutant''' | '''Structure of the MoaA Arg17/266/268/Ala triple mutant''' | ||
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[[Category: Haenzelmann, P.]] | [[Category: Haenzelmann, P.]] | ||
[[Category: Schindelin, H.]] | [[Category: Schindelin, H.]] | ||
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Revision as of 00:40, 4 May 2008
Structure of the MoaA Arg17/266/268/Ala triple mutant
Overview
The first step in molybdenum cofactor biosynthesis, the conversion of 5'-GTP to precursor Z, an oxygen-sensitive tetrahydropyranopterin is catalyzed by the S-adenosylmethionine (SAM)-dependent enzyme MoaA and the accessory protein MoaC. This reaction involves the radical-initiated intramolecular rearrangement of the guanine C8 atom. MoaA harbors an N-terminal [4Fe-4S] cluster, which is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical (5'-dA*), and a C-terminal [4Fe-4S] cluster presumably involved in substrate binding and/or activation. Biochemical studies identified residues involved in 5'-GTP binding and the determinants of nucleotide specificity. The crystal structure of MoaA in complex with 5'-GTP confirms the biochemical data and provides valuable insights into the subsequent radical reaction. MoaA binds 5'-GTP with high affinity and interacts through its C-terminal [4Fe-4S] cluster with the guanine N1 and N2 atoms, in a yet uncharacterized binding mode. The tightly anchored triphosphate moiety prevents the escape of radical intermediates. This structure also visualizes the L-Met and 5'-dA cleavage products of SAM. Rotation of the 5'-dA ribose and/or conformational changes of the guanosine are proposed to bring the 5'-deoxyadenosyl radical into close proximity of either the ribose C2' and C3' or the guanine C8 carbon atoms leading to hydrogen abstraction.
About this Structure
2FB2 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
Binding of 5'-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism., Hanzelmann P, Schindelin H, Proc Natl Acad Sci U S A. 2006 May 2;103(18):6829-34. Epub 2006 Apr 21. PMID:16632608 Page seeded by OCA on Sun May 4 03:40:46 2008
