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000207454 1001_ $$0P:(DE-HGF)0$$aSyson, Karl$$b0$$eCorresponding Author
000207454 245__ $$aStructural Insight into How Streptomyces coelicolor Maltosyl Transferase GlgE Binds $\alpha$-Maltose 1-Phosphate and Forms a Maltosyl-Enzyme Intermediate
000207454 260__ $$aColumbus, Ohio$$bAmerican Chemical Society$$c2014
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000207454 520__ $$aGlgE (EC 2.4.99.16) is an α-maltose 1-phosphate:(1→4)-α- D -glucan 4-α- D -maltosyltransferase of theCAZy glycoside hydrolase 13_3 family. It is the definingenzyme of a bacterial α-glucan biosynthetic pathway and is agenetically validated anti-tuberculosis target. It catalyzes the α-retaining transfer of maltosyl units from α-maltose 1-phosphate to maltooligosaccharides and is predicted to use adouble-displacement mechanism. Evidence of this mechanismwas obtained using a combination of site-directed mutagenesis of Streptomyces coelicolor GlgE isoform I, substrate analogues,protein crystallography, and mass spectrometry. The X-ray structures of α-maltose 1-phosphate bound to a D394A mutein and aβ-2-deoxy-2-fluoromaltosyl-enzyme intermediate with a E423A mutein were determined. There are few examples of CAZyglycoside hydrolase family 13 members that have had their glycosyl-enzyme intermediate structures determined, and none beforenow have been obtained with a 2-deoxy-2-fluoro substrate analogue. The covalent modification of Asp394 was confirmed usingmass spectrometry. A similar modification of wild-type GlgE proteins from S. coelicolor and Mycobacterium tuberculosis was alsoobserved. Small-angle X-ray scattering of the M. tuberculosis enzyme revealed a homodimeric assembly similar to that of the S.coelicolor enzyme but with slightly differently oriented monomers. The deeper understanding of the structure−functionrelationships of S. coelicolor GlgE will aid the development of inhibitors of the M. tuberculosis enzyme.
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000207454 536__ $$0G:(EU-Grant)226716$$aELISA - European Light Sources Activities - Synchrotrons and Free Electron Lasers (226716)$$c226716$$fFP7-INFRASTRUCTURES-2008-1$$x1
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000207454 7001_ $$0P:(DE-HGF)0$$aStevenson, Clare E. M.$$b1
000207454 7001_ $$0P:(DE-HGF)0$$aRashid, Abdul M.$$b2
000207454 7001_ $$0P:(DE-HGF)0$$aSaalbach, Gerhard$$b3
000207454 7001_ $$0P:(DE-HGF)0$$aTang, Minhong$$b4
000207454 7001_ $$0P:(DE-H253)PIP1016657$$aTuukkanen, Anne$$b5
000207454 7001_ $$0P:(DE-H253)PIP1001422$$aSvergun, Dmitri$$b6
000207454 7001_ $$0P:(DE-HGF)0$$aWithers, Stephen G.$$b7
000207454 7001_ $$0P:(DE-HGF)0$$aLawson, David M.$$b8
000207454 7001_ $$0P:(DE-HGF)0$$aBornemann, Stephen$$b9
000207454 773__ $$0PERI:(DE-600)1472258-6$$a10.1021/bi500183c$$gVol. 53, no. 15, p. 2494 - 2504$$n15$$p2494 - 2504$$tBiochemistry$$v53$$x1520-4995$$y2014
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