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| - | [[Image:2fb2.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2fb2| PDB=2fb2 | SCENE= }} | | {{STRUCTURE_2fb2| PDB=2fb2 | SCENE= }} |
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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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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_16632608}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16632608 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16632608}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: S-adenosylmethionine]] | | [[Category: S-adenosylmethionine]] |
| | [[Category: Tim barrel]] | | [[Category: Tim barrel]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:40:46 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:06:17 2008'' |
Revision as of 03:06, 28 July 2008
Template:STRUCTURE 2fb2
Structure of the MoaA Arg17/266/268/Ala triple mutant
Template:ABSTRACT PUBMED 16632608
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 Mon Jul 28 06:06:17 2008
