5OJV

Crystal structure of Mycolicibacterium hassiacum glucosylglycerate hydrolase (MhGgH) E419A variant in complex with mannosylglycerate

Summary for 5OJV

• Entry DOI: 10.2210/pdb5ojv/pdb
• Descriptor: Uncharacterized protein, GLYCEROL, (2R)-3-hydroxy-2-(alpha-D-mannopyranosyloxy)propanoic acid, ... (5 entities in total)
• Functional Keywords: mycobacterium, hydrolase
• Biological source: Mycobacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
• Total number of polymer chains: 2
• Total formula weight: 103269.30

Authors

Cereija, T.B.,Macedo-Ribeiro, S.,Pereira, P.J.B. (deposition date: 2017-07-24, release date: 2018-08-08, Last modification date: 2024-01-17)

Primary citation

Cereija, T.B.,Alarico, S.,Lourenco, E.C.,Manso, J.A.,Ventura, M.R.,Empadinhas, N.,Macedo-Ribeiro, S.,Pereira, P.J.B.
The structural characterization of a glucosylglycerate hydrolase provides insights into the molecular mechanism of mycobacterial recovery from nitrogen starvation.
Iucrj, 6:572-585, 2019

PubMed Abstract: Bacteria are challenged to adapt to environmental variations in order to survive. Under nutritional stress, several bacteria are able to slow down their metabolism into a nonreplicating state and wait for favourable conditions. It is almost universal that bacteria accumulate carbon stores to survive during this nonreplicating state and to fuel rapid proliferation when the growth-limiting stress disappears. Mycobacteria are exceedingly successful in their ability to become dormant under harsh circumstances and to be able to resume growth when conditions are favourable. Rapidly growing mycobacteria accumulate glucosylglycerate under nitrogen-limiting conditions and quickly mobilize it when nitrogen availability is restored. The depletion of intracellular glucosyl-glycerate levels in (basonym ) was associated with the up-regulation of the gene coding for glucosylglycerate hydrolase (GgH), an enzyme that is able to hydrolyse glucosylglycerate to glycerate and glucose, a source of readily available energy. Highly conserved among unrelated phyla, GgH is likely to be involved in bacterial reactivation following nitrogen starvation, which in addition to other factors driving mycobacterial recovery may also provide an opportunity for therapeutic intervention, especially in the serious infections caused by some emerging opportunistic pathogens of this group, such as (basonym ). Using a combination of biochemical methods and hybrid structural approaches, the oligomeric organization of GgH was determined and molecular determinants of its substrate binding and specificity were unveiled.

PubMed: 31316802
DOI: 10.1107/S2052252519005372

Experimental method

X-RAY DIFFRACTION (2.062 Å)