2fb3: Difference between revisions

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[[Image:2fb3.gif|left|200px]]<br /><applet load="2fb3" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2fb3.gif|left|200px]]
caption="2fb3, resolution 2.349&Aring;" />
 
'''Structure of MoaA in complex with 5'-GTP'''<br />
{{Structure
|PDB= 2fb3 |SIZE=350|CAPTION= <scene name='initialview01'>2fb3</scene>, resolution 2.349&Aring;
|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'-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=5AD:5'-DEOXYADENOSINE'>5AD</scene> and <scene name='pdbligand=POP:PYROPHOSPHATE 2-'>POP</scene>
|ACTIVITY=
|GENE= MoaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
}}
 
'''Structure of MoaA in complex with 5'-GTP'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2FB3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=MET:'>MET</scene>, <scene name='pdbligand=SF4:'>SF4</scene>, <scene name='pdbligand=GTP:'>GTP</scene>, <scene name='pdbligand=5AD:'>5AD</scene> and <scene name='pdbligand=POP:'>POP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FB3 OCA].  
2FB3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FB3 OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16632608 16632608]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16632608 16632608]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: 5'-deoxyadenosine]]
[[Category: 5'-deoxyadenosine]]
[[Category: 5'-gtp]]
[[Category: 5'-gtp]]
[[Category: [4fe-4s] clusters]]
[[Category: [4fe-4s] cluster]]
[[Category: s-adenosylmethionine]]
[[Category: s-adenosylmethionine]]
[[Category: tim barrel]]
[[Category: tim barrel]]


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Revision as of 17:50, 20 March 2008

File:2fb3.gif


PDB ID 2fb3

Drag the structure with the mouse to rotate
, resolution 2.349Å
Ligands: , , , , and
Gene: MoaA (Staphylococcus aureus)
Coordinates: save as pdb, mmCIF, xml



Structure of MoaA in complex with 5'-GTP


OverviewOverview

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 StructureAbout this Structure

2FB3 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

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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