PDBsum entry 4cyd

Transcription

PDB id: 4cyd

Contents

Protein chains

223 a.a.

21 a.a.

20 a.a.

Ligands

CMP ×4

GOL ×2

Waters ×409

PDB id:

4cyd

Name:

Transcription

Title:

Glxr bound to camp

Structure:

Probable transcription regulator. Chain: a, b, c, d. Fragment: residues 3-227. Synonym: glxr. Engineered: yes. Probable expression tag. Chain: f, h. Engineered: yes

Source:

Corynebacterium glutamicum. Organism_taxid: 1718. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic construct. Organism_taxid: 32630. Expression_system_taxid: 562

Resolution:

1.82Å R-factor: 0.192 R-free: 0.246

Authors:

P.D.Townsend,M.Bott,M.J.Cann,E.Pohl

Key ref:

P.D.Townsend 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. PubMed id: 25469635 DOI: 10.1371/journal.pone.0113265

Date:

10-Apr-14 Release date: 17-Dec-14

Protein chains

H7C677  (H7C677_CORGT) -  Crp/Fnr family transcriptional regulator from Corynebacterium glutamicum

Seq: 227 a.a.

Struc: 223 a.a.

Protein chain

No UniProt id for this chain

Struc: 21 a.a.

Protein chain

No UniProt id for this chain

Struc: 20 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C, D: E.C.?

DOI no: 10.1371/journal.pone.0113265

Plos One 9:e113265 (2014)

PubMed id: 25469635

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.

P.D.Townsend, B.Jungwirth, F.Pojer, M.Bußmann, V.A.Money, S.T.Cole, A.Pühler, A.Tauch, M.Bott, M.J.Cann, E.Pohl.

ABSTRACT

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.