1n2c: Difference between revisions

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==Overview==

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.

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 Structure==

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[[Category: Protein complex]]

[[Category: Kisker, C.]]

[[Category: Rees, D.C.]]

[[Category: Rees, D C.]]

[[Category: Schindelin, H.]]

[[Category: ADP]]

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[[Category: signal transduction]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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 Structure==
@@ Line 15: / Line 15: @@
 [[Category: Protein complex]]
 [[Category: Kisker, C.]]
-[[Category: Rees, D.C.]]
+[[Category: Rees, D C.]]
 [[Category: Schindelin, H.]]
 [[Category: ADP]]
@@ Line 32: / Line 32: @@
 [[Category: signal transduction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:26:39 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:28 2008''