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Three-Dimensional Solution Structure of the Cyanide Adduct of a Variant of Saccharomyces cerevisiae Iso-1-cytochrome c Containing the Met80Ala Mutation. Identification of Ligand-Residue Interactions in the Distal Heme Cavity

Banci, Lucia and Bertini, Ivano and Bren, Kara L. and Gray, Harry B. and Sompornpisut, Pornthep and Turano, Paola (1995) Three-Dimensional Solution Structure of the Cyanide Adduct of a Variant of Saccharomyces cerevisiae Iso-1-cytochrome c Containing the Met80Ala Mutation. Identification of Ligand-Residue Interactions in the Distal Heme Cavity. Biochemistry, 34 (36). pp. 11385-11398. ISSN 0006-2960. doi:10.1021/bi00036a011. https://resolver.caltech.edu/CaltechAUTHORS:20180206-065819564

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Abstract

The ^1H NMR spectrum of the the cyanide adduct of a triply mutated Saccharomyces cerevisiae iso-1-cytochrome c (His39Gln/Met80Ala/CyslO2Seri)n the oxidized form has been assigned through 1D NOE and 2D COSY, TOCSY, NOESY, and NOE-NOESY experiments; 562 protons out of a total of 683 have been assigned. The solution structure, the first of a paramagnetic heme protein, was determined using 1426 meaningful NOE constraints out of a total of 1842 measured NOES. The RMSD values at the stage of restrained energy minimization of 17 structures obtained from distance geometry calculations are 0.68 ± 0.11 and 1.32 ± 0.14 Å for the backbone and all heavy atoms, respectively. The quality, in terms of RMSD, of the present structure is the same as that obtained for the solution structure of the diamagnetic horse heart ferrocytochrome c [Qi, P. X., et al. (1994) Biochemistry 33, 6408-64191. The secondary structure elements and the overall folding in the variant are observed to be the same as those of the wild-type protein for which the X-ray structure is available. However, the replacement of the methionine axial ligand with an alanine residue creates a ligand-binding “distal cavity.” The properties of the distal cavity seen in this solution structure are compared to those of other heme proteins.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/bi00036a011DOIArticle
https://pubs.acs.org/doi/abs/10.1021/bi00036a011PublisherArticle
https://pubs.acs.org/doi/suppl/10.1021/bi00036a011PublisherSupporting Information
ORCID:
AuthorORCID
Gray, Harry B.0000-0002-7937-7876
Turano, Paola0000-0002-7683-8614
Additional Information:© 1995 American Chemical Society. Published in print 12 September 1995. We thank Yi Lu for helpful discussions. K.L.B. acknowledges a Kodak graduate fellowship. P.S. acknowledges the Italian Ministry of Foreign Affairs for a Ph.D. grant. This work was supported by the EC Biotechnology Program BI02-CT94-2052 (DG12SSMA), the CNR (Italy), and the National Science Foundation (United States). This work has been performed with the instrumentation of the Florence Laboratory of Relaxometry and Magnetic Resonance on Paramagnetic Metalloproteins, Large Scale Facility of the European Community.
Funders:
Funding AgencyGrant Number
KodakUNSPECIFIED
Ministero degli Affari EsteriUNSPECIFIED
European CommunityBI02-CT94-2052
Consiglio Nazionale delle Ricerche (CNR)UNSPECIFIED
NSFUNSPECIFIED
Issue or Number:36
DOI:10.1021/bi00036a011
Record Number:CaltechAUTHORS:20180206-065819564
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20180206-065819564
Official Citation:Three-Dimensional Solution Structure of the Cyanide Adduct of a Variant of Saccharomyces cerevisiae Iso-1-cytochrome c Containing the Met80Ala Mutation. Identification of Ligand-Residue Interactions in the Distal Heme Cavity Lucia Banci, Ivano Bertini, Kara L. Bren, Harry B. Gray, Pornthep Sompornpisut, and Paola Turano Biochemistry 1995 34 (36), 11385-11398 DOI: 10.1021/bi00036a011
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:84680
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:06 Feb 2018 19:02
Last Modified:15 Nov 2021 20:21

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