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| | <StructureSection load='5ohz' size='340' side='right'caption='[[5ohz]], [[Resolution|resolution]] 2.04Å' scene=''> | | <StructureSection load='5ohz' size='340' side='right'caption='[[5ohz]], [[Resolution|resolution]] 2.04Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ohz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mychd Mychd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OHZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OHZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ohz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_hassiacum_DSM_44199 Mycolicibacterium hassiacum DSM 44199]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OHZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OHZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.036Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=2CO:S-HYDROPEROXYCYSTEINE'>2CO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2CO:S-HYDROPEROXYCYSTEINE'>2CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C731_0006 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1122247 MYCHD])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ohz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ohz OCA], [https://pdbe.org/5ohz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ohz RCSB], [https://www.ebi.ac.uk/pdbsum/5ohz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ohz ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ohz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ohz OCA], [http://pdbe.org/5ohz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ohz RCSB], [http://www.ebi.ac.uk/pdbsum/5ohz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ohz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/GGH_MYCHD GGH_MYCHD] Catalyzes the hydrolysis of glucosylglycerate (GG) to glycerate and glucose (PubMed:25341489, PubMed:31316802). Involved in recovery from nitrogen starvation by promoting the rapid mobilization of the glucosylglycerate that accumulates under these conditions (PubMed:25341489). Can also hydrolyze mannosylglycerate (MG), with tenfold lower efficiency (PubMed:31316802).<ref>PMID:25341489</ref> <ref>PMID:31316802</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mychd]] | + | [[Category: Mycolicibacterium hassiacum DSM 44199]] |
| - | [[Category: Cereija, T B]] | + | [[Category: Cereija TB]] |
| - | [[Category: Macedo-Ribeiro, S]] | + | [[Category: Macedo-Ribeiro S]] |
| - | [[Category: Pereira, P J.B]] | + | [[Category: Pereira PJB]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Mycobacterium]]
| + | |
| Structural highlights
Function
GGH_MYCHD Catalyzes the hydrolysis of glucosylglycerate (GG) to glycerate and glucose (PubMed:25341489, PubMed:31316802). Involved in recovery from nitrogen starvation by promoting the rapid mobilization of the glucosylglycerate that accumulates under these conditions (PubMed:25341489). Can also hydrolyze mannosylglycerate (MG), with tenfold lower efficiency (PubMed:31316802).[1] [2]
Publication Abstract from PubMed
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.
The structural characterization of a glucosylglycerate hydrolase provides insights into the molecular mechanism of mycobacterial recovery from nitrogen starvation.,Cereija TB, Alarico S, Lourenco EC, Manso JA, Ventura MR, Empadinhas N, Macedo-Ribeiro S, Pereira PJB IUCrJ. 2019 May 8;6(Pt 4):572-585. doi: 10.1107/S2052252519005372. eCollection, 2019 Jul 1. PMID:31316802[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Alarico S, Costa M, Sousa MS, Maranha A, Lourenço EC, Faria TQ, Ventura MR, Empadinhas N. Mycobacterium hassiacum recovers from nitrogen starvation with up-regulation of a novel glucosylglycerate hydrolase and depletion of the accumulated glucosylglycerate. Sci Rep. 2014 Oct 24;4:6766. PMID:25341489 doi:10.1038/srep06766
- ↑ Cereija TB, Alarico S, Lourenco EC, Manso JA, Ventura MR, Empadinhas N, Macedo-Ribeiro S, Pereira PJB. The structural characterization of a glucosylglycerate hydrolase provides insights into the molecular mechanism of mycobacterial recovery from nitrogen starvation. IUCrJ. 2019 May 8;6(Pt 4):572-585. doi: 10.1107/S2052252519005372. eCollection, 2019 Jul 1. PMID:31316802 doi:http://dx.doi.org/10.1107/S2052252519005372
- ↑ Cereija TB, Alarico S, Lourenco EC, Manso JA, Ventura MR, Empadinhas N, Macedo-Ribeiro S, Pereira PJB. The structural characterization of a glucosylglycerate hydrolase provides insights into the molecular mechanism of mycobacterial recovery from nitrogen starvation. IUCrJ. 2019 May 8;6(Pt 4):572-585. doi: 10.1107/S2052252519005372. eCollection, 2019 Jul 1. PMID:31316802 doi:http://dx.doi.org/10.1107/S2052252519005372
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