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| | <StructureSection load='5cj5' size='340' side='right'caption='[[5cj5]], [[Resolution|resolution]] 3.13Å' scene=''> | | <StructureSection load='5cj5' size='340' side='right'caption='[[5cj5]], [[Resolution|resolution]] 3.13Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cj5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myct3 Myct3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CJ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CJ5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5cj5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_thermoresistibile_ATCC_19527 Mycolicibacterium thermoresistibile ATCC 19527]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CJ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CJ5 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glgE, KEK_12948 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1078020 MYCT3])</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]] 3.13Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Starch_synthase_(maltosyl-transferring) Starch synthase (maltosyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.99.16 2.4.99.16] </span></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=5cj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cj5 OCA], [https://pdbe.org/5cj5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cj5 RCSB], [https://www.ebi.ac.uk/pdbsum/5cj5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cj5 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=5cj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cj5 OCA], [http://pdbe.org/5cj5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cj5 RCSB], [http://www.ebi.ac.uk/pdbsum/5cj5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cj5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/G7CL00_MYCTH G7CL00_MYCTH]] Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.[HAMAP-Rule:MF_02124] | + | [https://www.uniprot.org/uniprot/G7CL00_MYCT3 G7CL00_MYCT3] Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.[HAMAP-Rule:MF_02124] |
| | <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: Myct3]] | + | [[Category: Mycolicibacterium thermoresistibile ATCC 19527]] |
| - | [[Category: Blaszczyk, M]] | + | [[Category: Blaszczyk M]] |
| - | [[Category: Blundell, T L]] | + | [[Category: Blundell TL]] |
| - | [[Category: Empadinhas, N]] | + | [[Category: Empadinhas N]] |
| - | [[Category: Maranha, A]] | + | [[Category: Maranha A]] |
| - | [[Category: Mendes, V]] | + | [[Category: Mendes V]] |
| - | [[Category: Gh13]]
| + | |
| - | [[Category: Glge]]
| + | |
| - | [[Category: Maltose]]
| + | |
| - | [[Category: Maltosyltransferase]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
G7CL00_MYCT3 Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.[HAMAP-Rule:MF_02124]
Publication Abstract from PubMed
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.
Structure of Mycobacterium thermoresistibile GlgE defines novel conformational states that contribute to the catalytic mechanism.,Mendes V, Blaszczyk M, Maranha A, Empadinhas N, Blundell TL Sci Rep. 2015 Nov 30;5:17144. doi: 10.1038/srep17144. PMID:26616850[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mendes V, Blaszczyk M, Maranha A, Empadinhas N, Blundell TL. Structure of Mycobacterium thermoresistibile GlgE defines novel conformational states that contribute to the catalytic mechanism. Sci Rep. 2015 Nov 30;5:17144. doi: 10.1038/srep17144. PMID:26616850 doi:http://dx.doi.org/10.1038/srep17144
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