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Nitrogenase Complexes: Multiple Docking Sites for a Nucleotide Switch Protein

Tezcan, F. Akif and Kaiser, Jens T. and Mustafi, Debarshi and Walton, Mika Y. and Howard, James B. and Rees, Douglas C. (2005) Nitrogenase Complexes: Multiple Docking Sites for a Nucleotide Switch Protein. Science, 309 (5739). pp. 1377-1380. ISSN 0036-8075. doi:10.1126/science.1115653. https://resolver.caltech.edu/CaltechAUTHORS:20141121-144257412

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Abstract

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.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1126/science.1115653DOIArticle
http://www.sciencemag.org/content/309/5739/1377PublisherArticle
http://www.sciencemag.org/content/309/5739/1377/suppl/DC1PublisherSupporting Information
ORCID:
AuthorORCID
Tezcan, F. Akif0000-0002-4733-6500
Kaiser, Jens T.0000-0002-5948-5212
Rees, Douglas C.0000-0003-4073-1185
Additional Information:© 2005 American Association for the Advancement of Science. 2 June 2005; Accepted 1 August 2005. This work was supported by the NIH and HHMI. F.A.T. acknowledges the Helen Hay Whitney Foundation for a postdoctoral fellowship. Operations at Stanford Synchrotron Radiation Laboratory and the Advanced Light Source are funded by the Office of Basic Energy Sciences of the U.S. Department of Energy and NIH. We thank the Parsons and Moore Foundations for support of facilities at Caltech. Coordinates and structure factors for the nf-Av2:Av1, adp-Av2:Av1, and pcp-Av2:Av1 structures have been deposited in the RCSB Protein Data Bank (entries 2AFH, 2AFI, and 2AFK, respectively) for release upon publication.
Funders:
Funding AgencyGrant Number
NIHUNSPECIFIED
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
Helen Hay Whitney FoundationUNSPECIFIED
Department of Energy (DOE)UNSPECIFIED
Parsons FoundationUNSPECIFIED
Gordon and Betty Moore FoundationUNSPECIFIED
Issue or Number:5739
DOI:10.1126/science.1115653
Record Number:CaltechAUTHORS:20141121-144257412
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20141121-144257412
Official Citation:Tezcan, F. A., Kaiser, J. T., Mustafi, D., Walton, M. Y., Howard, J. B., & Rees, D. C. (2005). Nitrogenase Complexes: Multiple Docking Sites for a Nucleotide Switch Protein. Science, 309(5739), 1377-1380. doi: 10.1126/science.1115653
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:52057
Collection:CaltechAUTHORS
Deposited By: Joanne McCole
Deposited On:21 Nov 2014 23:21
Last Modified:10 Nov 2021 19:20

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