1rw4: Difference between revisions

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New page: left|200px<br /><applet load="1rw4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rw4, resolution 2.5Å" /> '''Nitrogenase Fe protei...
 
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[[Image:1rw4.jpg|left|200px]]<br /><applet load="1rw4" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1rw4.jpg|left|200px]]<br /><applet load="1rw4" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1rw4, resolution 2.5&Aring;" />
caption="1rw4, resolution 2.5&Aring;" />
'''Nitrogenase Fe protein l127 deletion variant'''<br />
'''Nitrogenase Fe protein l127 deletion variant'''<br />


==Overview==
==Overview==
The crystal structure of a nitrogenase Fe protein single site deletion, variant reveals a distinctly new conformation of the Fe protein and, indicates that, upon binding of MgATP, the Fe protein undergoes a dramatic, conformational change that is largely manifested in the rigid-body, reorientation of the homodimeric Fe protein subunits with respect to one, another. The observed conformational state allows the rationalization of a, model of structurally and chemically complementary interactions that occur, upon initial complex formation with the MoFe protein component that are, distinct from the protein-protein interactions that have been, characterized previously for stabilized nitrogenase complexes. The, crystallographic results, in combination with complementary UV-visible, absorption, EPR, and resonance Raman spectroscopic data, indicate that the, [4Fe-4S] cluster of both the Fe protein deletion variant and the native Fe, protein in the presence of MgATP can reversibly cycle between a regular, cubane-type [4Fe-4S] cluster in the reduced state and a cleaved form, involving two [2Fe-2S] fragments in the oxidized state. Resonance Raman, studies indicate that this novel cluster conversion is induced by, glycerol, and the crystallographic data suggest that glycerol is bound as, a bridging bidentate ligand to both [2Fe-2S] cluster fragments in the, oxidized state.
The crystal structure of a nitrogenase Fe protein single site deletion variant reveals a distinctly new conformation of the Fe protein and indicates that, upon binding of MgATP, the Fe protein undergoes a dramatic conformational change that is largely manifested in the rigid-body reorientation of the homodimeric Fe protein subunits with respect to one another. The observed conformational state allows the rationalization of a model of structurally and chemically complementary interactions that occur upon initial complex formation with the MoFe protein component that are distinct from the protein-protein interactions that have been characterized previously for stabilized nitrogenase complexes. The crystallographic results, in combination with complementary UV-visible absorption, EPR, and resonance Raman spectroscopic data, indicate that the [4Fe-4S] cluster of both the Fe protein deletion variant and the native Fe protein in the presence of MgATP can reversibly cycle between a regular cubane-type [4Fe-4S] cluster in the reduced state and a cleaved form involving two [2Fe-2S] fragments in the oxidized state. Resonance Raman studies indicate that this novel cluster conversion is induced by glycerol, and the crystallographic data suggest that glycerol is bound as a bridging bidentate ligand to both [2Fe-2S] cluster fragments in the oxidized state.


==About this Structure==
==About this Structure==
1RW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with SF4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RW4 OCA].  
1RW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RW4 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Igarashi, R.]]
[[Category: Igarashi, R.]]
[[Category: Johnson, M.K.]]
[[Category: Johnson, M K.]]
[[Category: Peters, J.W.]]
[[Category: Peters, J W.]]
[[Category: Seefeldt, L.C.]]
[[Category: Seefeldt, L C.]]
[[Category: Sen, S.]]
[[Category: Sen, S.]]
[[Category: Smith, A.]]
[[Category: Smith, A.]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]


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