2jhe | pdb_00002jhe

N-TERMINAL DOMAIN OF TYRR TRANSCRIPTION FACTOR (RESIDUES 1 -190)

spinqualitylabelsall models 2jhe, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jhe is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. Ligands: AE3, PG4, SO4 Activity: Glucokinase, with EC number 2.7.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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.,Verger D, Carr PD, Kwok T, Ollis DL J Mol Biol. 2007 Mar 16;367(1):102-12. Epub 2006 Dec 12. PMID:17222426 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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