2fb3

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|PDB= 2fb3 |SIZE=350|CAPTION= <scene name='initialview01'>2fb3</scene>, resolution 2.349&Aring;
|PDB= 2fb3 |SIZE=350|CAPTION= <scene name='initialview01'>2fb3</scene>, resolution 2.349&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=GTP:GUANOSINE-5&#39;-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=5AD:5&#39;-DEOXYADENOSINE'>5AD</scene> and <scene name='pdbligand=POP:PYROPHOSPHATE 2-'>POP</scene>
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|LIGAND= <scene name='pdbligand=5AD:5&#39;-DEOXYADENOSINE'>5AD</scene>, <scene name='pdbligand=GTP:GUANOSINE-5&#39;-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= MoaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
|GENE= MoaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
 +
|DOMAIN=
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|RELATEDENTRY=[[1tv7|1TV7]], [[2fb2|2FB2]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fb3 OCA], [http://www.ebi.ac.uk/pdbsum/2fb3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fb3 RCSB]</span>
}}
}}
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[[Category: Haenzelmann, P.]]
[[Category: Haenzelmann, P.]]
[[Category: Schindelin, H.]]
[[Category: Schindelin, H.]]
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[[Category: 5AD]]
 
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[[Category: GTP]]
 
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[[Category: MET]]
 
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[[Category: POP]]
 
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[[Category: SF4]]
 
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[[Category: SO4]]
 
[[Category: 5'-deoxyadenosine]]
[[Category: 5'-deoxyadenosine]]
[[Category: 5'-gtp]]
[[Category: 5'-gtp]]
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[[Category: tim barrel]]
[[Category: tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:04:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:00:18 2008''

Revision as of 00:00, 31 March 2008


PDB ID 2fb3

Drag the structure with the mouse to rotate
, resolution 2.349Å
Ligands: , , , , ,
Gene: MoaA (Staphylococcus aureus)
Related: 1TV7, 2FB2


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Structure of MoaA in complex with 5'-GTP


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

2FB3 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[[Category: [4fe-4s] cluster]]

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