View source for 4u98


==Structure of mycobacterial maltokinase, the missing link in the essential GlgE-pathway (AppCp complex)==
<StructureSection load='4u98' size='340' side='right'caption='[[4u98]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4u98]] 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=4U98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U98 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4u98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u98 OCA], [https://pdbe.org/4u98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u98 RCSB], [https://www.ebi.ac.uk/pdbsum/4u98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u98 ProSAT]</span></td></tr>
</table>
== Function ==
[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;">
== 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<ref>PMID:25619172</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4u98" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycolicibacterium vanbaalenii PYR-1]]
[[Category: Empadinhas N]]
[[Category: Fraga J]]
[[Category: Macedo-Ribeiro S]]
[[Category: Pereira PJB]]