4eib: Difference between revisions
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==Crystal Structure of Circular Permuted CBM21 (CP90) Gives Insight into the Altered Selectivity on Carbohydrate Binding.== | |||
<StructureSection load='4eib' size='340' side='right' caption='[[4eib]], [[Resolution|resolution]] 1.86Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4eib]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhizopus_oryzae Rhizopus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EIB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EIB FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">amyA, CBM21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=64495 Rhizopus oryzae])</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=4eib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eib OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eib RCSB], [http://www.ebi.ac.uk/pdbsum/4eib PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glucoamylases, containing starch-binding domains (SBD), have a wide range of scientific and industrial applications. Random mutagenesis and DNA shuffling of the gene encoding a starch-binding domain have resulted in only minor improvements in the affinities of the corresponding protein to their ligands, whereas circular permutation of the RoCBM21 substantially improved its binding affinity and selectivity towards longer-chain carbohydrates. For the study reported herein, we used a standard soluble ligand (amylose EX-I) to characterize the functional and structural aspects of circularly permuted RoCBM21 (CP90). Site-directed mutagenesis and the analysis of crystal structure reveal the dimerisation and an altered binding path, which may be responsible for improved affinity and altered selectivity of this newly created starch-binding domain. The functional and structural characterization of CP90 suggests that it has significant potential in industrial applications. | |||
Crystal structure of circular permuted RoCBM21 (CP90): dimerisation and proximity of binding sites.,Stephen P, Cheng KC, Lyu PC PLoS One. 2012;7(11):e50488. doi: 10.1371/journal.pone.0050488. Epub 2012 Nov 30. PMID:23226294<ref>PMID:23226294</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Rhizopus oryzae]] | [[Category: Rhizopus oryzae]] | ||
[[Category: Cheng, K C | [[Category: Cheng, K C]] | ||
[[Category: Lyu, P C | [[Category: Lyu, P C]] | ||
[[Category: Stephen, P | [[Category: Stephen, P]] | ||
[[Category: Amylose]] | [[Category: Amylose]] | ||
[[Category: Beta barrel]] | [[Category: Beta barrel]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Starch binding]] | [[Category: Starch binding]] | ||
Revision as of 14:45, 21 December 2014
Crystal Structure of Circular Permuted CBM21 (CP90) Gives Insight into the Altered Selectivity on Carbohydrate Binding.Crystal Structure of Circular Permuted CBM21 (CP90) Gives Insight into the Altered Selectivity on Carbohydrate Binding.
Structural highlights
Publication Abstract from PubMedGlucoamylases, containing starch-binding domains (SBD), have a wide range of scientific and industrial applications. Random mutagenesis and DNA shuffling of the gene encoding a starch-binding domain have resulted in only minor improvements in the affinities of the corresponding protein to their ligands, whereas circular permutation of the RoCBM21 substantially improved its binding affinity and selectivity towards longer-chain carbohydrates. For the study reported herein, we used a standard soluble ligand (amylose EX-I) to characterize the functional and structural aspects of circularly permuted RoCBM21 (CP90). Site-directed mutagenesis and the analysis of crystal structure reveal the dimerisation and an altered binding path, which may be responsible for improved affinity and altered selectivity of this newly created starch-binding domain. The functional and structural characterization of CP90 suggests that it has significant potential in industrial applications. Crystal structure of circular permuted RoCBM21 (CP90): dimerisation and proximity of binding sites.,Stephen P, Cheng KC, Lyu PC PLoS One. 2012;7(11):e50488. doi: 10.1371/journal.pone.0050488. Epub 2012 Nov 30. PMID:23226294[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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