5e9a: Difference between revisions
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==Crsytal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3== | |||
<StructureSection load='5e9a' size='340' side='right' caption='[[5e9a]], [[Resolution|resolution]] 2.56Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5e9a]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E9A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E9A 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=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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=5e9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e9a OCA], [http://pdbe.org/5e9a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e9a RCSB], [http://www.ebi.ac.uk/pdbsum/5e9a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e9a ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A novel gene was isolated for the first time from a psychrophilic gram-negative bacterium Rahnella sp. R3. The gene encoded a cold-adapted beta-galactosidase (R-beta-Gal). Recombinant R-beta-Gal was expressed in Escherichia coli BL21 (DE3), purified and characterized. R-beta-gal belongs to the glycosyl hydrolase family 42. Circular dichroism spectrometry of the structural stability of R-beta-Gal with respect to temperature indicated that the secondary structures of the enzyme were stable to 45 degrees C. In solution, the enzyme was a homo-trimer and was active at temperatures as low as 4 degrees C. The enzyme did not require the presence of metal ions to be active, but Mg(2+), Mn(2+), and Ca(2+) enhanced its activity slightly, whereas Fe(3+), Zn(2+) and Al(3+) appeared to inactive it. The purified enzyme displayed K(m) values of 6.5 mM for ONPG and 2.2mM for lactose at 4 degrees C. These values were lower than the corresponding K(m)s reported for other cold-adapted beta-Gals. | |||
Cloning, expression and structural stability of a cold-adapted beta-galactosidase from Rahnella sp. R3.,Fan Y, Hua X, Zhang Y, Feng Y, Shen Q, Dong J, Zhao W, Zhang W, Jin Z, Yang R Protein Expr Purif. 2015 Nov;115:158-64. doi: 10.1016/j.pep.2015.07.001. Epub, 2015 Jul 3. PMID:26145832<ref>PMID:26145832</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Fan, Y | <div class="pdbe-citations 5e9a" style="background-color:#fffaf0;"></div> | ||
[[Category: Zhang, Y | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Beta-galactosidase]] | |||
[[Category: Fan, Y T]] | |||
[[Category: Zhang, Y Z]] | |||
[[Category: Galactosidase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Lactose]] | |||
[[Category: Tim barrel]] | |||
Revision as of 21:25, 26 October 2016
Crsytal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3Crsytal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3
Structural highlights
Publication Abstract from PubMedA novel gene was isolated for the first time from a psychrophilic gram-negative bacterium Rahnella sp. R3. The gene encoded a cold-adapted beta-galactosidase (R-beta-Gal). Recombinant R-beta-Gal was expressed in Escherichia coli BL21 (DE3), purified and characterized. R-beta-gal belongs to the glycosyl hydrolase family 42. Circular dichroism spectrometry of the structural stability of R-beta-Gal with respect to temperature indicated that the secondary structures of the enzyme were stable to 45 degrees C. In solution, the enzyme was a homo-trimer and was active at temperatures as low as 4 degrees C. The enzyme did not require the presence of metal ions to be active, but Mg(2+), Mn(2+), and Ca(2+) enhanced its activity slightly, whereas Fe(3+), Zn(2+) and Al(3+) appeared to inactive it. The purified enzyme displayed K(m) values of 6.5 mM for ONPG and 2.2mM for lactose at 4 degrees C. These values were lower than the corresponding K(m)s reported for other cold-adapted beta-Gals. Cloning, expression and structural stability of a cold-adapted beta-galactosidase from Rahnella sp. R3.,Fan Y, Hua X, Zhang Y, Feng Y, Shen Q, Dong J, Zhao W, Zhang W, Jin Z, Yang R Protein Expr Purif. 2015 Nov;115:158-64. doi: 10.1016/j.pep.2015.07.001. Epub, 2015 Jul 3. PMID:26145832[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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