1rw4
From Proteopedia
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| - | [[Image:1rw4.jpg|left|200px]] | + | [[Image:1rw4.jpg|left|200px]] |
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| - | '''Nitrogenase Fe protein l127 deletion variant''' | + | {{Structure |
| + | |PDB= 1rw4 |SIZE=350|CAPTION= <scene name='initialview01'>1rw4</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= nifH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=354 Azotobacter vinelandii]) | ||
| + | }} | ||
| + | |||
| + | '''Nitrogenase Fe protein l127 deletion variant''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RW4 is a [ | + | 1RW4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RW4 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14967020 14967020] |
[[Category: Azotobacter vinelandii]] | [[Category: Azotobacter vinelandii]] | ||
[[Category: Nitrogenase]] | [[Category: Nitrogenase]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:57:01 2008'' |
Revision as of 11:57, 20 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | nifH (Azotobacter vinelandii) | ||||||
| Activity: | Nitrogenase, with EC number 1.18.6.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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