PDBsum entry 5ohc

Hydrolase

PDB id: 5ohc

Contents

Protein chains

445 a.a.

Ligands

GOL ×10

Waters ×705

PDB id:

5ohc

Name:

Hydrolase

Title:

Crystal structure of mycolicibacterium hassiacum glucosylglycerate hydrolase (mhggh) in complex with glycerol

Structure:

Hydrolase. Chain: a, b. Engineered: yes

Source:

Mycobacterium hassiacum (strain dsm 44199 / cip 105218 / jcm 12690 / 3849). Organism_taxid: 1122247. Gene: c731_0006. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.00Å R-factor: 0.169 R-free: 0.210

Authors:

T.B.Cereija,S.Macedo-Ribeiro,P.J.B.Pereira

Key ref:

T.B.Cereija et al. (2019). The structural characterization of a glucosylglycerate hydrolase provides insights into the molecular mechanism of mycobacterial recovery from nitrogen starvation. IUCrJ, 6, 572-585. PubMed id: 31316802 DOI: 10.1107/S2052252519005372

Date:

14-Jul-17 Release date: 01-Aug-18

Protein chains

K5BDL0  (GGH_MYCHD) -  Glucosylglycerate hydrolase from Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)

Seq: 446 a.a.

Struc: 445 a.a.

Enzyme reactions

• Enzyme class: E.C.3.2.1.208 - glucosylglycerate hydrolase.
• Reaction: (2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + H2O = (R)-glycerate + D-glucose

(2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + H2O = (R)-glycerate (Bound ligand (Het Group name = GOL) matches with 85.71% similarity) + D-glucose

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1107/S2052252519005372

IUCrJ 6:572-585 (2019)

PubMed id: 31316802

The structural characterization of a glucosylglycerate hydrolase provides insights into the molecular mechanism of mycobacterial recovery from nitrogen starvation.

T.B.Cereija, S.Alarico, E.C.Lourenço, J.A.Manso, M.R.Ventura, N.Empadinhas, S.Macedo-Ribeiro, P.J.B.Pereira.

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 Mycolicibacterium hassiacum (basonym Mycobacterium hassiacum) 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 Mycobacteroides abscessus (basonym Mycobacterium abscessus). Using a combination of biochemical methods and hybrid structural approaches, the oligomeric organization of M. hassiacum GgH was determined and molecular determinants of its substrate binding and specificity were unveiled.