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==CPF_2247, a novel alpha-amylase from Clostridium perfringens== | |||
===CPF_2247, | <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 [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3REN FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1502 Clostridium perfringens])</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=3ren FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ren OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ren RCSB], [http://www.ebi.ac.uk/pdbsum/3ren PDBsum]</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> | |||
==See Also== | ==See Also== | ||
*[[Amylase|Amylase]] | *[[Amylase|Amylase]] | ||
*[[User:Gabriel Pons/Sandbox 2|User:Gabriel Pons/Sandbox 2]] | |||
== | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Clostridium perfringens]] | [[Category: Clostridium perfringens]] | ||
[[Category: Boraston, A B | [[Category: Boraston, A B]] | ||
[[Category: Ficko-Blean, E | [[Category: Ficko-Blean, E]] | ||
[[Category: Stuart, C P | [[Category: Stuart, C P]] | ||
[[Category: Alpha-amylase]] | [[Category: Alpha-amylase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 13:58, 19 December 2014
CPF_2247, a novel alpha-amylase from Clostridium perfringensCPF_2247, a novel alpha-amylase from Clostridium perfringens
Structural highlights
Publication Abstract from PubMedCPF_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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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