This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 15: | Line 15: | ||
[[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
|
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
Page seeded by OCA on Thu Feb 21 14:55:08 2008
