3ren: Difference between revisions
Jump to navigation
Jump to search
New page: '''Unreleased structure''' The entry 3ren is ON HOLD Authors: Ficko-Blean, E., Stuart, C.P., Boraston, A.B. Description: CPF_2247, a novel alpha-amylase from Clostridium perfringens |
No edit summary |
||
| (11 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==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/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 [https://proteopedia.org/fgij/fg.htm?mol=3REN FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0H2YP60_CLOP1 A0A0H2YP60_CLOP1] | |||
<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== | |||
*[[Amylase 3D structures|Amylase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Clostridium perfringens]] | |||
[[Category: Large Structures]] | |||
[[Category: Boraston AB]] | |||
[[Category: Ficko-Blean E]] | |||
[[Category: Stuart CP]] | |||
Latest revision as of 13:23, 6 November 2024
CPF_2247, a novel alpha-amylase from Clostridium perfringensCPF_2247, a novel alpha-amylase from Clostridium perfringens
Structural highlights
FunctionPublication 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
|
| ||||||||||||||||||