1n2c: Difference between revisions
New page: left|200px<br /> <applet load="1n2c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n2c, resolution 3.0Å" /> '''NITROGENASE COMPLEX ... |
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[[Image:1n2c. | [[Image:1n2c.jpg|left|200px]]<br /><applet load="1n2c" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1n2c, resolution 3.0Å" /> | caption="1n2c, resolution 3.0Å" /> | ||
'''NITROGENASE COMPLEX FROM AZOTOBACTER VINELANDII STABILIZED BY ADP-TETRAFLUOROALUMINATE'''<br /> | '''NITROGENASE COMPLEX FROM AZOTOBACTER VINELANDII STABILIZED BY ADP-TETRAFLUOROALUMINATE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1N2C 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 CA, MG, ALF, HCA, CFM, CLF, SF4 and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1N2C with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb26_1.html Nitrogenase]]. 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:// | 1N2C 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=ALF:'>ALF</scene>, <scene name='pdbligand=HCA:'>HCA</scene>, <scene name='pdbligand=CFM:'>CFM</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]. The following page contains interesting information on the relation of 1N2C with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb26_1.html Nitrogenase]]. 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=1N2C OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
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Revision as of 17:26, 15 February 2008
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NITROGENASE COMPLEX FROM AZOTOBACTER VINELANDII STABILIZED BY ADP-TETRAFLUOROALUMINATE
OverviewOverview
The coupling of ATP hydrolysis to electron transfer by the enzyme, nitrogenase during biological nitrogen fixation is an important example of, a nucleotide-dependent transduction mechanism. The crystal structure has, been determined for the complex between the Fe-protein and MoFe-protein, components of nitrogenase stabilized by ADP x AIF4-, previously used as a, nucleoside triphosphate analogue in nucleotide-switch proteins. The, structure reveals that the dimeric Fe-protein has undergone substantial, conformational changes. The beta-phosphate and AIF4- groups are stabilized, through intersubunit contacts that are critical for catalysis and the, redox centre is repositioned to facilitate electron transfer. Interactions, in the nitrogenase complex have broad implications for signal and energy, transduction mechanisms in multiprotein complexes.
About this StructureAbout this Structure
1N2C is a Protein complex structure of sequences from Azotobacter vinelandii with , , , , , , and as ligands. The following page contains interesting information on the relation of 1N2C with [Nitrogenase]. Active as Nitrogenase, with EC number 1.18.6.1 Full crystallographic information is available from OCA.
ReferenceReference
Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction., Schindelin H, Kisker C, Schlessman JL, Howard JB, Rees DC, Nature. 1997 May 22;387(6631):370-6. PMID:9163420
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