3bue

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Crystal structure of the C-terminal domain hexamer of ArgR from Mycobacterium tuberculosisCrystal structure of the C-terminal domain hexamer of ArgR from Mycobacterium tuberculosis

Structural highlights

3bue is a 6 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Cherney LT, Cherney MM, Garen CR, Lu GJ, James MN. Structure of the C-terminal domain of the arginine repressor protein from Mycobacterium tuberculosis. Acta Crystallogr D Biol Crystallogr. 2008 Sep;64(Pt 9):950-6. Epub 2008, Aug 13. PMID:18703843 doi:http://dx.doi.org/10.1107/S0907444908021513

3bue, resolution 2.15Å

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