Journalartikel - Artikel | 2014 | Peer reviewed

The Crystal Structures of Apo and cAMP-Bound GlxR from Corynebacterium glutamicum Reveal Structural and Dynamic Changes upon cAMP Binding in CRP/FNR Family Transcription Factors

Autor(en)

Townsend, Philip D. ; Jungwirth, Britta ; Pojer, Florence ; Bußmann, Michael ; Money, Victoria A. ; Cole, Stewart T. ; Pühler, Alfred ; Tauch, Andreas ; Bott, Michael ; Cann, Martin J. ; Pohl, Ehmke

Normierter Zeitschriftentitel

PLOS ONE

DOI

10.1371/journal.pone.0113265

PubMed-ID

25469635

URL

https://pub.uni-bielefeld.de/record/2710114

Web of Science-ID

000349128700019

Weitere Details

Sprache

englisch

Darstellungsform

Text

Band

Artikelnummer

e113265

Ausgabe

The cyclic AMP-dependent transcriptional regulator GlxR from Corynebacterium glutamicum is a member of the super-family of CRP/FNR (cyclic AMP receptor protein/fumarate and nitrate reduction regulator) transcriptional regulators that play central roles in bacterial metabolic regulatory networks. In C. glutamicum, which is widely used for the industrial production of amino acids and serves as a non-pathogenic model organism for members of the Corynebacteriales including Mycobacterium tuberculosis, the GlxR homodimer controls the transcription of a large number of genes involved in carbon metabolism. GlxR therefore represents a key target for understanding the regulation and coordination of C. glutamicum metabolism. Here we investigate cylic AMP and DNA binding of GlxR from C. glutamicum and describe the crystal structures of apo GlxR determined at a resolution of 2.5 Å, and two crystal forms of holo GlxR at resolutions of 2.38 and 1.82 Å, respectively. The detailed structural analysis and comparison of GlxR with CRP reveals that the protein undergoes a distinctive conformational change upon cyclic AMP binding leading to a dimer structure more compatible to DNA-binding. As the two binding sites in the GlxR homodimer are structurally identical dynamic changes upon binding of the first ligand are responsible for the allosteric behavior. The results presented here show how dynamic and structural changes in GlxR lead to optimization of orientation and distance of its two DNA-binding helices for optimal DNA recognition.

Zitierstile

Townsend PD, Jungwirth B, Pojer F, et al. The Crystal Structures of Apo and cAMP-Bound GlxR from Corynebacterium glutamicum Reveal Structural and Dynamic Changes upon cAMP Binding in CRP/FNR Family Transcription Factors. PloS one. 2014;9(12): e113265.

In die Zwischenablage einfügen

Townsend, P. D., Jungwirth, B., Pojer, F., Bußmann, M., Money, V. A., Cole, S. T., Pühler, A., et al. (2014). The Crystal Structures of Apo and cAMP-Bound GlxR from Corynebacterium glutamicum Reveal Structural and Dynamic Changes upon cAMP Binding in CRP/FNR Family Transcription Factors. PloS one, 9(12), e113265. doi:10.1371/journal.pone.0113265

In die Zwischenablage einfügen

Townsend, Philip D, Jungwirth, Britta, Pojer, Florence, Bußmann, Michael, Money, Victoria A, Cole, Stewart T, Pühler, Alfred, et al. 2014. “The Crystal Structures of Apo and cAMP-Bound GlxR from Corynebacterium glutamicum Reveal Structural and Dynamic Changes upon cAMP Binding in CRP/FNR Family Transcription Factors”. PloS one 9 (12): e113265.

In die Zwischenablage einfügen

Townsend, P. D., Jungwirth, B., Pojer, F., Bußmann, M., Money, V. A., Cole, S. T., Pühler, A., Tauch, A., Bott, M., Cann, M. J., et al. (2014). The Crystal Structures of Apo and cAMP-Bound GlxR from Corynebacterium glutamicum Reveal Structural and Dynamic Changes upon cAMP Binding in CRP/FNR Family Transcription Factors. PloS one 9:e113265.

In die Zwischenablage einfügen

Townsend, P.D., et al., 2014. The Crystal Structures of Apo and cAMP-Bound GlxR from Corynebacterium glutamicum Reveal Structural and Dynamic Changes upon cAMP Binding in CRP/FNR Family Transcription Factors. PloS one, 9(12): e113265.

In die Zwischenablage einfügen

P.D. Townsend, et al., “The Crystal Structures of Apo and cAMP-Bound GlxR from Corynebacterium glutamicum Reveal Structural and Dynamic Changes upon cAMP Binding in CRP/FNR Family Transcription Factors”, PloS one, vol. 9, 2014, : e113265.

In die Zwischenablage einfügen

Townsend, P.D., Jungwirth, B., Pojer, F., Bußmann, M., Money, V.A., Cole, S.T., Pühler, A., Tauch, A., Bott, M., Cann, M.J., Pohl, E.: The Crystal Structures of Apo and cAMP-Bound GlxR from Corynebacterium glutamicum Reveal Structural and Dynamic Changes upon cAMP Binding in CRP/FNR Family Transcription Factors. PloS one. 9, : e113265 (2014).

In die Zwischenablage einfügen

Townsend, Philip D, Jungwirth, Britta, Pojer, Florence, Bußmann, Michael, Money, Victoria A, Cole, Stewart T, Pühler, Alfred, Tauch, Andreas, Bott, Michael, Cann, Martin J, and Pohl, Ehmke. “The Crystal Structures of Apo and cAMP-Bound GlxR from Corynebacterium glutamicum Reveal Structural and Dynamic Changes upon cAMP Binding in CRP/FNR Family Transcription Factors”. PloS one 9.12 (2014): e113265.

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