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| | <StructureSection load='4wzy' size='340' side='right'caption='[[4wzy]], [[Resolution|resolution]] 1.71Å' scene=''> | | <StructureSection load='4wzy' size='340' side='right'caption='[[4wzy]], [[Resolution|resolution]] 1.71Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wzy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycvp Mycvp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WZY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WZY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wzy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_vanbaalenii_PYR-1 Mycolicibacterium vanbaalenii PYR-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WZY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WZY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u94|4u94]], [[4u98|4u98]]</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=4wzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wzy OCA], [https://pdbe.org/4wzy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wzy RCSB], [https://www.ebi.ac.uk/pdbsum/4wzy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wzy ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mak, Mvan_5735 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=350058 MYCVP])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Maltokinase Maltokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.175 2.7.1.175] </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=4wzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wzy OCA], [http://pdbe.org/4wzy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wzy RCSB], [http://www.ebi.ac.uk/pdbsum/4wzy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wzy ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MAK_MYCVP MAK_MYCVP]] Catalyzes the ATP-dependent phosphorylation of maltose to maltose 1-phosphate. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, GlgE and GlgB (By similarity). | + | [https://www.uniprot.org/uniprot/MAK_MYCVP MAK_MYCVP] Catalyzes the ATP-dependent phosphorylation of maltose to maltose 1-phosphate. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, GlgE and GlgB (By similarity). |
| | <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: Maltokinase]] | + | [[Category: Mycolicibacterium vanbaalenii PYR-1]] |
| - | [[Category: Mycvp]]
| + | [[Category: Empadinhas N]] |
| - | [[Category: Empadinhas, N]] | + | [[Category: Fraga J]] |
| - | [[Category: Fraga, J]] | + | [[Category: Macedo-Ribeiro S]] |
| - | [[Category: Macedo-Ribeiro, S]] | + | [[Category: Pereira PJB]] |
| - | [[Category: Pereira, P J.B]] | + | |
| - | [[Category: Atp]]
| + | |
| - | [[Category: Glycogen]]
| + | |
| - | [[Category: Maltose]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
MAK_MYCVP Catalyzes the ATP-dependent phosphorylation of maltose to maltose 1-phosphate. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, GlgE and GlgB (By similarity).
Publication Abstract from PubMed
A novel four-step pathway identified recently in mycobacteria channels trehalose to glycogen synthesis and is also likely involved in the biosynthesis of two other crucial polymers: intracellular methylglucose lipopolysaccharides and exposed capsular glucan. The structures of three of the intervening enzymes - GlgB, GlgE, and TreS - were recently reported, providing the first templates for rational drug design. Here we describe the structural characterization of the fourth enzyme of the pathway, mycobacterial maltokinase (Mak), uncovering a eukaryotic-like kinase (ELK) fold, similar to methylthioribose kinases and aminoglycoside phosphotransferases. The 1.15 A structure of Mak in complex with a non-hydrolysable ATP analog reveals subtle structural rearrangements upon nucleotide binding in the cleft between the N- and the C-terminal lobes. Remarkably, this new family of ELKs has a novel N-terminal domain topologically resembling the cystatin family of protease inhibitors. By interfacing with and restraining the mobility of the phosphate-binding region of the N-terminal lobe, Mak's unusual N-terminal domain might regulate its phosphotransfer activity and represents the most likely anchoring point for TreS, the upstream enzyme in the pathway. By completing the gallery of atomic-detail models of an essential pathway, this structure opens new avenues for the rational design of alternative anti-tubercular compounds.
Structure of mycobacterial maltokinase, the missing link in the essential GlgE-pathway.,Fraga J, Maranha A, Mendes V, Pereira PJ, Empadinhas N, Macedo-Ribeiro S Sci Rep. 2015 Jan 26;5:8026. doi: 10.1038/srep08026. PMID:25619172[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fraga J, Maranha A, Mendes V, Pereira PJ, Empadinhas N, Macedo-Ribeiro S. Structure of mycobacterial maltokinase, the missing link in the essential GlgE-pathway. Sci Rep. 2015 Jan 26;5:8026. doi: 10.1038/srep08026. PMID:25619172 doi:http://dx.doi.org/10.1038/srep08026
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