Predicted structure of the sugar-binding site of the lac repressor
- Select a language for the TTS:
- UK English Female
- UK English Male
- US English Female
- US English Male
- Australian Female
- Australian Male
- Language selected: (auto detect) - EN
Play all audios:

ABSTRACT The lactose repressor protein from _Escherichia coli_ binds sugars, primarily galactosides, which modulate its interactions with operator DNA and thereby affect synthesis of the
_lac_ metabolic enzymes1. The affinity of the repressor for operator DNA is decreased by binding inducer sugars and increased by binding anti-inducer sugars2. Based on regions of the primary
structure implicated by genetic methods to be involved in sugar binding3–5, amino acid sequence homology between L-arabinose-binding protein (ABP) and _lac_ repressor has recently been
reported6. The sugar-binding sites for these two proteins might be expected to have similar structural features, as both bind L-arabinose and D-galactose. The high resolution structure of
ABP reported in the accompanying article7 provides complete definition of amino acids in the sugar-binding site. By identification of homologous residues in the _lac_ repressor, we have now
predicted the structure of the portion of the repressor sugar-binding site which accommodates the galactosyl moiety. This prediction provides the first potential view of the
inducer/anti-inducer site in the repressor protein. Access through your institution Buy or subscribe This is a preview of subscription content, access via your institution ACCESS OPTIONS
Access through your institution Subscribe to this journal Receive 51 print issues and online access $199.00 per year only $3.90 per issue Learn more Buy this article * Purchase on
SpringerLink * Instant access to full article PDF Buy now Prices may be subject to local taxes which are calculated during checkout ADDITIONAL ACCESS OPTIONS: * Log in * Learn about
institutional subscriptions * Read our FAQs * Contact customer support SIMILAR CONTENT BEING VIEWED BY OTHERS STRUCTURAL ANALYSIS AND INSIGHT INTO EFFECTOR BINDING OF THE NIACIN-RESPONSIVE
REPRESSOR NIAR FROM _BACILLUS HALODURANS_ Article Open access 03 December 2020 MECHANISM OF NANR GENE REPRESSION AND ALLOSTERIC INDUCTION OF BACTERIAL SIALIC ACID METABOLISM Article Open
access 31 March 2021 X-RAY CRYSTALLOGRAPHY REVEALS MOLECULAR RECOGNITION MECHANISM FOR SUGAR BINDING IN A MELIBIOSE TRANSPORTER MELB Article Open access 02 August 2021 REFERENCES * Miller,
J. H. & Reznikoff, W. S. _The Operon_ (Cold Spring Harbor Laboratory, New York, 1979). Google Scholar * Barkley, M. D., Riggs, A. D., Jobe, A. & Bourgeois, S. _Biochemistry_ 14,
1700–1712 (1975). Article CAS Google Scholar * Pfahl, M., Stockter, C. & Gronenborn, B. _Genetics_ 76, 669–679 (1974). CAS PubMed PubMed Central Google Scholar * Miller, J. H. _J.
molec. Biol._ 131, 249–258 (1979). Article CAS Google Scholar * Müller-Hill, B., Gronenborn, B., Kania, J., Schlotmann, M. & Beyreuther, K. in _Nucleic Acid-Protein Recognition_ (ed.
Vogel, H. J.) 219–236 (Academic, New York, 1977). Book Google Scholar * Müller-Hill, B. _Nature_ 302, 163–164 (1983). Article ADS Google Scholar * Quiocho, F. A. & Vyas, N. K.
_Nature_ 310, 381–386 (1984). Article ADS CAS Google Scholar * Newcomer, M. E., Gilliland, G. L. & Quiocho, F. A. _J. biol. Chem._ 256, 13213–13217 (1981). CAS PubMed Google
Scholar * Platt, T., Files, J. G. & Weber, K. _J. biol. Chem._ 248, 110–121 (1973). CAS PubMed Google Scholar * Matthews, K. S. _J. biol. Chem._ 254, 3348–3353 (1979). CAS PubMed
Google Scholar * Miller, J. H. _et al._ _J. molec. Biol._ 131, 191–222 (1979). Article CAS Google Scholar * Müller-Hill, B., Rickenberg, H. V. & Wallenfels, K. _J. molec. Biol._ 10,
303–318 (1964). Article Google Scholar * Newcomer, M. E., Lewis, B. A. & Quiocho, F. A. _J. biol. Chem._ 256, 13218–13222 (1981). CAS PubMed Google Scholar * Matthews, K. S.
_Biochim. biophys. Acta_ 359, 334–340 (1974). Article CAS Google Scholar * Laiken, S. L., Gross, C. A. & von Hippel, P. H. _J. molec. Biol._ 66, 143–155 (1972). Article CAS Google
Scholar * Yang, D. S., Burgum, A. A. & Matthews, K. S. _Biochim. biophys. Acta_ 493, 24–36 (1977). Article CAS Google Scholar * Alexander, M. E., Burgum, A. A., Noall, R. A., Shaw,
M. D. & Matthews, K. S. _Biochim. biophys. Acta_ 493, 367–379 (1977). Article CAS Google Scholar * O'Gorman, R. B. & Matthews, K. S. _J. biol. Chem._ 252, 3565–3571 (1977).
CAS PubMed Google Scholar * Boschelli, F., Jarema, M. A. C. & Lu, P. _J. biol. Chem._ 256, 11595–11599 (1981). CAS PubMed Google Scholar * Jarema, M. A. C., Lu, P. & Miller, J.
H. _Proc. natn. Acad. Sci. U.S.A._ 78, 2707–2711 (1981). Article ADS CAS Google Scholar * Fries, D. C., Rao, S. T. & Sundaralingam, M. _Acta crystallogr._ B27, 994–1005 (1971).
Article CAS Google Scholar * Kanters, J. A., Roelofsen, G., Doesburg, H. M. & Koops, T. _Acta crystallogr._ B32, 2830–2837 (1976). Article Google Scholar Download references AUTHOR
INFORMATION AUTHORS AND AFFILIATIONS * Department of Biochemistry, Rice University, Houston, Texas, 77251, USA Clarence F. Sams, Nand K. Vyas, Florante A. Quiocho & Kathleen Shive
Matthews Authors * Clarence F. Sams View author publications You can also search for this author inPubMed Google Scholar * Nand K. Vyas View author publications You can also search for this
author inPubMed Google Scholar * Florante A. Quiocho View author publications You can also search for this author inPubMed Google Scholar * Kathleen Shive Matthews View author publications
You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Sams, C., Vyas, N., Quiocho, F. _et al._
Predicted structure of the sugar-binding site of the _lac_ repressor. _Nature_ 310, 429–430 (1984). https://doi.org/10.1038/310429a0 Download citation * Received: 09 January 1984 * Accepted:
10 May 1984 * Issue Date: 02 August 1984 * DOI: https://doi.org/10.1038/310429a0 SHARE THIS ARTICLE Anyone you share the following link with will be able to read this content: Get shareable
link Sorry, a shareable link is not currently available for this article. Copy to clipboard Provided by the Springer Nature SharedIt content-sharing initiative