4cn1
From Proteopedia
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| - | ''' | + | ==GlgE isoform 1 from Streptomyces coelicolor D394A mutant with maltose- 1-phosphate bound== |
| + | <StructureSection load='4cn1' size='340' side='right' caption='[[4cn1]], [[Resolution|resolution]] 2.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4cn1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CN1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CN1 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M1F:ALPHA-MALTOSE+1-PHOSPHATE'>M1F</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cn4|4cn4]], [[4cn6|4cn6]]</td></tr> | ||
| + | <tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cn1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cn1 RCSB], [http://www.ebi.ac.uk/pdbsum/4cn1 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | GlgE (EC 2.4.99.16) is an alpha-maltose 1-phosphate:(1-->4)-alpha-d-glucan 4-alpha-d-maltosyltransferase of the CAZy glycoside hydrolase 13_3 family. It is the defining enzyme of a bacterial alpha-glucan biosynthetic pathway and is a genetically validated anti-tuberculosis target. It catalyzes the alpha-retaining transfer of maltosyl units from alpha-maltose 1-phosphate to maltooligosaccharides and is predicted to use a double-displacement mechanism. Evidence of this mechanism was 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 alpha-maltose 1-phosphate bound to a D394A mutein and a beta-2-deoxy-2-fluoromaltosyl-enzyme intermediate with a E423A mutein were determined. There are few examples of CAZy glycoside hydrolase family 13 members that have had their glycosyl-enzyme intermediate structures determined, and none before now have been obtained with a 2-deoxy-2-fluoro substrate analogue. The covalent modification of Asp394 was confirmed using mass spectrometry. A similar modification of wild-type GlgE proteins from S. coelicolor and Mycobacterium tuberculosis was also observed. 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-function relationships of S. coelicolor GlgE will aid the development of inhibitors of the M. tuberculosis enzyme. | ||
| - | + | Structural Insight into How Streptomyces coelicolor Maltosyl Transferase GlgE Binds alpha-Maltose 1-Phosphate and Forms a Maltosyl-enzyme Intermediate.,Syson K, Stevenson CE, Rashid AM, Saalbach G, Tang M, Tuukkanen A, Svergun DI, Withers SG, Lawson DM, Bornemann S Biochemistry. 2014 Apr 22;53(15):2494-504. doi: 10.1021/bi500183c. Epub 2014 Apr , 11. PMID:24689960<ref>PMID:24689960</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bornemann, S.]] | ||
| + | [[Category: Lawson, D M.]] | ||
| + | [[Category: Rashid, A M.]] | ||
| + | [[Category: Saalbach, G.]] | ||
| + | [[Category: Stevenson, C E.M.]] | ||
| + | [[Category: Svergun, D I.]] | ||
| + | [[Category: Syson, K.]] | ||
| + | [[Category: Tang, M.]] | ||
| + | [[Category: Tuukanen, A.]] | ||
| + | [[Category: Withers, S G.]] | ||
| + | [[Category: Alpha-glucan biosynthesis]] | ||
| + | [[Category: Drug target]] | ||
| + | [[Category: Glycoside hydrolase family 13_3]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 09:09, 21 May 2014
GlgE isoform 1 from Streptomyces coelicolor D394A mutant with maltose- 1-phosphate bound
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