PDBsum entry 2jhe

Transcription

PDB id

2jhe

Contents

			Protein chains

					189 a.a.

			Ligands

					AE3


					PG4 ×2


					SO4

			Waters ×146

References listed in PDB file

Key reference

Title

Crystal structure of the n-Terminal domain of the tyrr transcription factor responsible for gene regulation of aromatic amino acid biosynthesis and transport in escherichia coli k12.

Authors

D.Verger, P.D.Carr, T.Kwok, D.L.Ollis.

Ref.

J Mol Biol, 2007, 367, 102-112. [DOI no: 10.1016/j.jmb.2006.12.018]

PubMed id

17222426

Abstract

The X-ray structure of the N-terminal domain of TyrR has been solved to a resolution of 2.3 A. It reveals a modular protein containing an ACT domain, a connecting helix, a PAS domain and a C-terminal helix. Two dimers are present in the asymmetric unit with one monomer of each pair exhibiting a large rigid-body movement that results in a hinging around residue 74 of approximately 50 degrees . The structure of the dimer is discussed with reference to other transcription regulator proteins. Putative binding sites are identified for the aromatic amino acid cofactors.



	Figure 2. Figure 2. Selected views of a TyrR^NT dimer. (a) The view highlights the extension of the N-terminal ACT domains into a single eight-stranded sheet flanked on one side by antiparallel helices. (b) The view in (a) rotated around the NCS dyad relating the two N-terminal ACT domains. This view shows the rotation of the NCS dyad that relates the rest of the molecule to its dimer equivalent chain with respect to the first dyad. The B chain (blue) clearly shows four sub-domains; the N-terminal ACT domain, the connecting helix, the PAS domain, and the final C-terminal helix. (c) A topology diagram of a monomer of TyrR showing the separate domains. (d) The original view rotated 90° to look down on the N-terminal domains showing the twofold relationship between the monomers. (e) Looking from below at the C-terminal end of the molecule, the arrow indicates the direction of the view, i.e. along the second NCS dyad axis relating the PAS domains and the C-terminal helices. (f) The same view with the final C-terminal helix removed from each chain to give a clearer view of the PAS domains and connecting helices. Figure 2. Selected views of a TyrR^NT dimer. (a) The view highlights the extension of the N-terminal ACT domains into a single eight-stranded sheet flanked on one side by antiparallel helices. (b) The view in (a) rotated around the NCS dyad relating the two N-terminal ACT domains. This view shows the rotation of the NCS dyad that relates the rest of the molecule to its dimer equivalent chain with respect to the first dyad. The B chain (blue) clearly shows four sub-domains; the N-terminal ACT domain, the connecting helix, the PAS domain, and the final C-terminal helix. (c) A topology diagram of a monomer of TyrR showing the separate domains. (d) The original view rotated 90° to look down on the N-terminal domains showing the twofold relationship between the monomers. (e) Looking from below at the C-terminal end of the molecule, the arrow indicates the direction of the view, i.e. along the second NCS dyad axis relating the PAS domains and the C-terminal helices. (f) The same view with the final C-terminal helix removed from each chain to give a clearer view of the PAS domains and connecting helices.		Figure 3. Figure 3. Overlay of the individual monomers of TyrR^NT. The N-terminal domains (residues 1–68) were superimposed. (left) A and B overlaid to show the conformational differences between monomers of the same dimer. (centre) A and C overlaid to show similarity of equivalent domains between dimers. (right) All four chains overlaid to show the full range of rigid body displacements. Figure 3. Overlay of the individual monomers of TyrR^NT. The N-terminal domains (residues 1–68) were superimposed. (left) A and B overlaid to show the conformational differences between monomers of the same dimer. (centre) A and C overlaid to show similarity of equivalent domains between dimers. (right) All four chains overlaid to show the full range of rigid body displacements.

PROCHECK

	Headers