2afi: Difference between revisions

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[[Image:2afi.gif|left|200px]]<br /><applet load="2afi" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2afi.gif|left|200px]]
caption="2afi, resolution 3.10&Aring;" />
 
'''Crystal Structure of MgADP bound Av2-Av1 Complex'''<br />
{{Structure
|PDB= 2afi |SIZE=350|CAPTION= <scene name='initialview01'>2afi</scene>, resolution 3.10&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=CFN:FE(7)-MO-S(9)-N+CLUSTER'>CFN</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</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=
}}
 
'''Crystal Structure of MgADP bound Av2-Av1 Complex'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2AFI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=HCA:'>HCA</scene>, <scene name='pdbligand=CFN:'>CFN</scene>, <scene name='pdbligand=CLF:'>CLF</scene>, <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=ADP:'>ADP</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=2AFI OCA].  
2AFI is a [[Protein complex]] structure of sequences 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=2AFI OCA].  


==Reference==
==Reference==
Nitrogenase complexes: multiple docking sites for a nucleotide switch protein., Tezcan FA, Kaiser JT, Mustafi D, Walton MY, Howard JB, Rees DC, Science. 2005 Aug 26;309(5739):1377-80. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16123301 16123301]
Nitrogenase complexes: multiple docking sites for a nucleotide switch protein., Tezcan FA, Kaiser JT, Mustafi D, Walton MY, Howard JB, Rees DC, Science. 2005 Aug 26;309(5739):1377-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16123301 16123301]
[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
[[Category: Nitrogenase]]
[[Category: Nitrogenase]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]


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Revision as of 16:49, 20 March 2008

File:2afi.gif


PDB ID 2afi

Drag the structure with the mouse to rotate
, resolution 3.10Å
Ligands: , , , , , and
Activity: Nitrogenase, with EC number 1.18.6.1
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of MgADP bound Av2-Av1 Complex


OverviewOverview

Adenosine triphosphate (ATP) hydrolysis in the nitrogenase complex controls the cycle of association and dissociation between the electron donor adenosine triphosphatase (ATPase) (Fe-protein) and its target catalytic protein (MoFe-protein), driving the reduction of dinitrogen into ammonia. Crystal structures in different nucleotide states have been determined that identify conformational changes in the nitrogenase complex during ATP turnover. These structures reveal distinct and mutually exclusive interaction sites on the MoFe-protein surface that are selectively populated, depending on the Fe-protein nucleotide state. A consequence of these different docking geometries is that the distance between redox cofactors, a critical determinant of the intermolecular electron transfer rate, is coupled to the nucleotide state. More generally, stabilization of distinct docking geometries by different nucleotide states, as seen for nitrogenase, could enable nucleotide hydrolysis to drive the relative motion of protein partners in molecular motors and other systems.

About this StructureAbout this Structure

2AFI is a Protein complex structure of sequences from Azotobacter vinelandii. Full crystallographic information is available from OCA.

ReferenceReference

Nitrogenase complexes: multiple docking sites for a nucleotide switch protein., Tezcan FA, Kaiser JT, Mustafi D, Walton MY, Howard JB, Rees DC, Science. 2005 Aug 26;309(5739):1377-80. PMID:16123301

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