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| | <StructureSection load='5jiw' size='340' side='right'caption='[[5jiw]], [[Resolution|resolution]] 1.73Å' scene=''> | | <StructureSection load='5jiw' size='340' side='right'caption='[[5jiw]], [[Resolution|resolution]] 1.73Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jiw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25104 Atcc 25104]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JIW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JIW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jiw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JIW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JIW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></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]] 1.73Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=271 ATCC 25104])</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=5jiw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jiw OCA], [https://pdbe.org/5jiw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jiw RCSB], [https://www.ebi.ac.uk/pdbsum/5jiw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jiw ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-alpha-glucanotransferase 4-alpha-glucanotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.25 2.4.1.25] </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=5jiw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jiw OCA], [http://pdbe.org/5jiw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jiw RCSB], [http://www.ebi.ac.uk/pdbsum/5jiw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jiw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MALQ_THETH MALQ_THETH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5jiw" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5jiw" style="background-color:#fffaf0;"></div> |
| - | | |
| - | ==See Also== | |
| - | *[[Amylose|Amylose]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 4-alpha-glucanotransferase]] | |
| - | [[Category: Atcc 25104]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bexten, N]] | + | [[Category: Thermus aquaticus]] |
| - | [[Category: Maier, T]] | + | [[Category: Bexten N]] |
| - | [[Category: Roth, C]] | + | [[Category: Maier T]] |
| - | [[Category: Saenger, T]] | + | [[Category: Roth C]] |
| - | [[Category: Straeter, N]] | + | [[Category: Saenger T]] |
| - | [[Category: Weizenmann, N]] | + | [[Category: Straeter N]] |
| - | [[Category: Zimmermann, W]] | + | [[Category: Weizenmann N]] |
| - | [[Category: Glycoside hydrolase]]
| + | [[Category: Zimmermann W]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Tim barrel cycloamylose]]
| + | |
| Structural highlights
5jiw is a 1 chain structure with sequence from Thermus aquaticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.73Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
MALQ_THETH
Publication Abstract from PubMed
Starch is a major carbon and energy source throughout all kingdoms of life. It consists of two carbohydrate polymers, branched amylopectin and linear amylose, which are sparingly soluble in water. Hence, the enzymatic breakdown by glycoside hydrolases (GHs) is of great biological and societal importance. Amylomaltases (AMs) are GHs specialized in the hydrolysis of alpha-1,4-linked sugar chains such as amylose. They are able to catalyze an intramolecular transglycosylation of a bound sugar chain yielding polymeric sugar rings, the cycloamyloses (CAs), consisting of 20 to 100 glucose units. Despite a wealth of data on short oligosaccharide binding to GHs, no structural evidence is available for their interaction with polymeric substrates that better represent the natural polysaccharide. We have determined the crystal structure of Thermus aquaticus AM in complex with a 34-meric CA-one of the largest carbohydrates resolved by x-ray crystallography and a mimic of the natural polymeric amylose substrate. In total, 15 glucose residues interact with the protein in an extended crevice with a length of more than 40 A. A modified succinimide, derived from aspartate, mediates protein-sugar interactions, suggesting a biological role for this nonstandard amino acid. The structure, together with functional assays, provides unique insights into the interaction of GHs with their polymeric substrate and reveals a molecular ruler mechanism for minimal ring-size determination of CA products.
Amylose recognition and ring-size determination of amylomaltase.,Roth C, Weizenmann N, Bexten N, Saenger W, Zimmermann W, Maier T, Strater N Sci Adv. 2017 Jan 13;3(1):e1601386. doi: 10.1126/sciadv.1601386. eCollection 2017, Jan. PMID:28097217[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Roth C, Weizenmann N, Bexten N, Saenger W, Zimmermann W, Maier T, Strater N. Amylose recognition and ring-size determination of amylomaltase. Sci Adv. 2017 Jan 13;3(1):e1601386. doi: 10.1126/sciadv.1601386. eCollection 2017, Jan. PMID:28097217 doi:http://dx.doi.org/10.1126/sciadv.1601386
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