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3ren
From Proteopedia
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| - | [[Image:3ren.png|left|200px]] | ||
| - | + | ==CPF_2247, a novel alpha-amylase from Clostridium perfringens== | |
| + | <StructureSection load='3ren' size='340' side='right'caption='[[3ren]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ren]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_perfringens"_veillon_and_zuber_1898 "bacillus perfringens" veillon and zuber 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3REN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3REN FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CPF_2247 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1502 "Bacillus perfringens" Veillon and Zuber 1898])</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=3ren FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ren OCA], [https://pdbe.org/3ren PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ren RCSB], [https://www.ebi.ac.uk/pdbsum/3ren PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ren ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | CPF_2247 from Clostridium perfringens ATCC 13124 was identified as a putative carbohydrate-active enzyme by its low sequence identity to endo-beta-1,4-glucanases belonging to family 8 of the glycoside hydrolase classification. The X-ray crystal structure of CPF_2247 determined to 2.0 A resolution by single-wavelength anomalous dispersion using seleno-methionine-substituted protein revealed an (alpha/alpha)(6) barrel fold. A large cleft on the surface of the protein contains residues that are structurally conserved with key elements of the catalytic machinery in clan GH-M glycoside hydrolases. Assessment of CPF_2247 as a carbohydrate-active enzyme disclosed alpha-glucanase activity on amylose, glycogen, and malto-oligosaccharides. | ||
| - | + | Structural analysis of CPF_2247, a novel alpha-amylase from Clostridium perfringens.,Ficko-Blean E, Stuart CP, Boraston AB Proteins. 2011 Oct;79(10):2771-7. doi: 10.1002/prot.23116. Epub 2011 Aug 26. PMID:21905105<ref>PMID:21905105</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3ren" style="background-color:#fffaf0;"></div> | |
==See Also== | ==See Also== | ||
| - | *[[ | + | *[[Amylase 3D structures|Amylase 3D structures]] |
| - | [[Category: | + | == References == |
| - | [[Category: Boraston, A B | + | <references/> |
| - | [[Category: Ficko-Blean, E | + | __TOC__ |
| - | [[Category: Stuart, C P | + | </StructureSection> |
| + | [[Category: Bacillus perfringens veillon and zuber 1898]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Boraston, A B]] | ||
| + | [[Category: Ficko-Blean, E]] | ||
| + | [[Category: Stuart, C P]] | ||
[[Category: Alpha-amylase]] | [[Category: Alpha-amylase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Current revision
CPF_2247, a novel alpha-amylase from Clostridium perfringens
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