1rw4

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|PDB= 1rw4 |SIZE=350|CAPTION= <scene name='initialview01'>1rw4</scene>, resolution 2.5&Aring;
|PDB= 1rw4 |SIZE=350|CAPTION= <scene name='initialview01'>1rw4</scene>, resolution 2.5&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>
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|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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE= nifH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=354 Azotobacter vinelandii])
|GENE= nifH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=354 Azotobacter vinelandii])
 +
|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rw4 OCA], [http://www.ebi.ac.uk/pdbsum/1rw4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rw4 RCSB]</span>
}}
}}
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[[Category: Sen, S.]]
[[Category: Sen, S.]]
[[Category: Smith, A.]]
[[Category: Smith, A.]]
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[[Category: GOL]]
 
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[[Category: SF4]]
 
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:57:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:33:46 2008''

Revision as of 20:33, 30 March 2008


PDB ID 1rw4

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands: ,
Gene: nifH (Azotobacter vinelandii)
Activity: Nitrogenase, with EC number 1.18.6.1
Resources: FirstGlance, OCA, PDBsum, RCSB
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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