5CJ5: Structure Of Mycobacterium Thermoresistibile Glge Apo Form At 3.13a Resolution

GlgE, an enzyme of the pathway that converts trehalose to alpha-glucans, is essential for Mycobacterium tuberculosis. Inhibition of GlgE, which transfers maltose from a maltose-1-phosphate donor to alpha-glucan/maltooligosaccharide chain acceptor, leads to a toxic accumulation of maltose-1-phosphate that culminates in cellular death. Here we describe the first high-resolution mycobacterial GlgE structure from Mycobacterium thermoresistibile at 1.96 A. We show that the structure resembles that of M. tuberculosis and Streptomyces coelicolor GlgEs, reported before, with each protomer in the homodimer comprising five domains. However, in M. thermoresistibile GlgE we observe several conformational states of the S domain and provide evidence that its high flexibility is important for enzyme activity. The structures here reported shed further light on the interactions between the N-terminal domains and the catalytic domains of opposing chains and how they contribute to the catalytic reaction. Importantly this work identifies a useful surrogate system to aid the development of GlgE inhibitors against opportunistic and pathogenic mycobacteria.
PDB ID: 5CJ5Download
MMDB ID: 134708
PDB Deposition Date: 2015/7/13
Updated in MMDB: 2015/12
Experimental Method:
x-ray diffraction
Resolution: 3.13  Å
Source Organism:
Similar Structures:
Biological Unit for 5CJ5: dimeric; determined by author and by software (PISA)
Molecular Components in 5CJ5
Label Count Molecule
Proteins (2 molecules)
Alpha-1,4-glucan:maltose-1-phosphate Maltosyltransferase
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB