1rw4
From Proteopedia
(New page: 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=" | + | [[Image:1rw4.jpg|left|200px]]<br /><applet load="1rw4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rw4, resolution 2.5Å" /> | caption="1rw4, resolution 2.5Å" /> | ||
'''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 | + | 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:// | + | 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 | + | [[Category: Johnson, M K.]] |
| - | [[Category: Peters, J | + | [[Category: Peters, J W.]] |
| - | [[Category: Seefeldt, L | + | [[Category: Seefeldt, L C.]] |
[[Category: Sen, S.]] | [[Category: Sen, S.]] | ||
[[Category: Smith, A.]] | [[Category: Smith, A.]] | ||
| Line 24: | Line 24: | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:08 2008'' |
Revision as of 12:55, 21 February 2008
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Nitrogenase Fe protein l127 deletion variant
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.
About this Structure
1RW4 is a Single protein structure of sequence from Azotobacter vinelandii with and as ligands. Active as Nitrogenase, with EC number 1.18.6.1 Full crystallographic information is available from OCA.
Reference
A conformational mimic of the MgATP-bound "on state" of the nitrogenase iron protein., Sen S, Igarashi R, Smith A, Johnson MK, Seefeldt LC, Peters JW, Biochemistry. 2004 Feb 24;43(7):1787-97. PMID:14967020
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