4ESQ

Crystal structure of the extracellular domain of PknH from Mycobacterium tuberculosis

Summary for 4ESQ

• Entry DOI: 10.2210/pdb4esq/pdb
• Descriptor: Serine/threonine protein kinase, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, TERBIUM(III) ION, ... (4 entities in total)
• Functional Keywords: receptor kinase, membrane, transferase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 21189.08

Authors

Cavazos, A.,Prigozhin, D.M.,Alber, T. (deposition date: 2012-04-23, release date: 2012-07-18, Last modification date: 2024-11-20)

Primary citation

Cavazos, A.,Prigozhin, D.M.,Alber, T.
Structure of the sensor domain of Mycobacterium tuberculosis PknH receptor kinase reveals a conserved binding cleft.
J.Mol.Biol., 422:488-494, 2012

PubMed Abstract: Since their discovery over 20 years ago, eukaryotic-like transmembrane receptor Ser/Thr protein kinases (STPKs) have been shown to play critical roles in the virulence, growth, persistence, and reactivation of many bacteria. Information regarding the signals transmitted by these proteins, however, remains scarce. To enhance understanding of the basis for STPK receptor signaling, we determined the 1.7-Å-resolution crystal structure of the extracellular sensor domain of the Mycobacterium tuberculosis receptor STPK, PknH (Rv1266c). The PknH sensor domain adopts an unanticipated fold containing two intramolecular disulfide bonds and a large hydrophobic and polar cleft. The residues lining the cleft and those surrounding the disulfide bonds are conserved. These results suggest that PknH binds a small-molecule ligand that signals by changing the location or quaternary structure of the kinase domain.

PubMed: 22727744
DOI: 10.1016/j.jmb.2012.06.011

Experimental method

X-RAY DIFFRACTION (1.7 Å)