3cag | pdb_00003cag

Crystal structure of the oligomerization domain hexamer of the arginine repressor protein from Mycobacterium tuberculosis in complex with 9 arginines.

spinqualitylabelsall models 3cag, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3cag is a 6 chain structure with sequence from Myctu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ARG Related: 2zfz, 3bue Gene: argR, ahrC, Rv1657, MT1695, MTCY06H11.22 (MYCTU) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ARGR_MYCTU] Regulates arginine biosynthesis genes (By similarity). 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 Mycobacterium tuberculosis (Mtb) gene product encoded by open reading frame Rv1657 is an arginine repressor (ArgR). All genes involved in the L-arginine (hereafter arginine) biosynthetic pathway are essential for optimal growth of the Mtb pathogen, thus making MtbArgR a potential target for drug design. The C-terminal domains of arginine repressors (CArgR) participate in oligomerization and arginine binding. Several crystal forms of CArgR from Mtb (MtbCArgR) have been obtained. The X-ray crystal structures of MtbCArgR were determined at 1.85 A resolution with bound arginine and at 2.15 A resolution in the unliganded form. These structures show that six molecules of MtbCArgR are arranged into a hexamer having approximate 32 point symmetry that is formed from two trimers. The trimers rotate relative to each other by about 11 degrees upon binding arginine. All residues in MtbCArgR deemed to be important for hexamer formation and for arginine binding have been identified from the experimentally determined structures presented. The hexamer contains six regular sites in which the arginine molecules have one common binding mode and three sites in which the arginine molecules have two overlapping binding modes. The latter sites only bind the ligand at high (200 mM) arginine concentrations. Structure of the C-terminal domain of the arginine repressor protein from Mycobacterium tuberculosis.,Cherney LT, Cherney MM, Garen CR, Lu GJ, James MN Acta Crystallogr D Biol Crystallogr. 2008 Sep;64(Pt 9):950-6. Epub 2008, Aug 13. PMID:18703843 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Arginine repressor 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA