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Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase

Chan, Michael K. and Mukund, Swarnalatha and Kletzin, Arnulf and Adams, Michael W. W. and Rees, Douglas C. (1995) Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science, 267 (5203). pp. 1463-1469. ISSN 0036-8075. doi:10.1126/science.7878465. https://resolver.caltech.edu/CaltechAUTHORS:20150121-112458293

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Abstract

The crystal structure of the tungsten-containing aldehyde ferredoxin oxidoreductase (AOR) from Pyrococcus furiosus, a hyperthermophilic archaeon (formerly archaebacterium) that grows optimally at 100 degrees C, has been determined at 2.3 angstrom resolution by means of multiple isomorphous replacement and multiple crystal form averaging. AOR consists of two identical subunits, each containing an Fe4S4 cluster and a molybdopterin-based tungsten cofactor that is analogous to the molybdenum cofactor found in a large class of oxotransferases. Whereas the general features of the tungsten coordination in this cofactor were consistent with a previously proposed structure, each AOR subunit unexpectedly contained two molybdopterin molecules that coordinate a tungsten by a total of four sulfur ligands, and the pterin system was modified by an intramolecular cyclization that generated a three-ringed structure. In comparison to other proteins, the hyperthermophilic enzyme AOR has a relatively small solvent-exposed surface area, and a relatively large number of both ion pairs and buried atoms. These properties may contribute to the extreme thermostability of this enzyme.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1126/science.7878465DOIArticle
http://www.sciencemag.org/content/267/5203/1463PublisherArticle
http://www.jstor.org/stable/2886539JSTORArticle
ORCID:
AuthorORCID
Rees, Douglas C.0000-0003-4073-1185
Additional Information:© 1995 American Association for the Advancement of Science. 30 September 1994; Accepted 20 January 1995. We thank B. T. Hsu, J. Schlessman, J. Kim, S. Faham, M. Stowell, and T. McPhillips for advice and assistance, and A. G. Myers, M. K. Johnson, P. J. Bjorkman, and J. E. Bercaw for discussions. Supported by USPHS grant GM50775 (D.C.R.); ONR grant N00014-90-J-1894 (M.W.W.A.), DOE grant FG09-88ER1 3901 (M.W.W.A.) and NSF grant BCS-9320069 (M.W.W.A.); the Beckman Institute, the Joseph Irvine Equipment Fund, and the Howard Hughes Medical Institute (to P. J. Bjorkman) for part of the diffraction instrumentation; NIH fellowship 1F32 GM1 5006 (M.K.C.); and by the rotation camera facility at the Stanford Synchrotron Radiation Laboratory, which in tum is supported by the Department of Energy, Office of Basic Energy Sciences, and the National Institutes of Health Biomedical Resource Technology Program, Division of Research Resources. Coordinates have been deposited in the Brookhaven Protein Data base, not yet available.
Funders:
Funding AgencyGrant Number
United States Public Health Service (USPHS)GM50775
Office of Naval Research (ONR)N00014-90-J-1894
Department of Energy (DOE)FG09-88ER13901
NSFBCS-9320069
Caltech Beckman InstituteUNSPECIFIED
Joseph Irvine Equipment FundUNSPECIFIED
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
NIH1F32 GM15006
Issue or Number:5203
DOI:10.1126/science.7878465
Record Number:CaltechAUTHORS:20150121-112458293
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150121-112458293
Official Citation:Chan, M., Mukund, S., Kletzin, A., Adams, M., & Rees, D. (1995). Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science, 267(5203), 1463-1469. doi: 10.1126/science.7878465
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:53944
Collection:CaltechAUTHORS
Deposited By: Joanne McCole
Deposited On:21 Jan 2015 20:32
Last Modified:10 Nov 2021 20:25

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