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The Structure of the ADP•AlF4- stabilized nitrogenase complex and its implications for signal transduction mechanism

Schindelin, Hermann and Kisker, Caroline and Schlessman, Jamie L. and Howard, James B. and Rees, Douglas C. (1997) The Structure of the ADP•AlF4- stabilized nitrogenase complex and its implications for signal transduction mechanism. Nature, 387 . pp. 370-376. ISSN 0028-0836. https://resolver.caltech.edu/CaltechAUTHORS:20150128-163948369

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Abstract

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·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 β-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.


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http://dx.doi.org/10.1038/387370a0DOIArticle
http://www.nature.com/nature/journal/v387/n6631/abs/387370a0.htmlPublisherArticle
http://rdcu.be/b6FzPublisherFree ReadCube access
ORCID:
AuthorORCID
Rees, Douglas C.0000-0003-4073-1185
Contact Email Address:phoebe@caltech.edu
Additional Information:© 1997 Nature Publishing Group. Received 5 December 1996; accepted 26 March 1997. Supported by the NIH (D.C.R. and J.B.H.), the NSF (J.B.H.) and by Deutsche Forschungsgemeinschaft postdoctoral fellowships (to C.K. and H.S.). X-PLOR calculations were performed on the CRAY C90 at the San Diego Supercomputer Center, supported by the NSF.
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Deposited On:08 Feb 2015 03:26
Last Modified:03 Oct 2019 07:56

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