3ta9: Difference between revisions
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[[ | ==beta-Glucosidase A from the halothermophile H. orenii== | ||
<StructureSection load='3ta9' size='340' side='right' caption='[[3ta9]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ta9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Halothermothrix_orenii Halothermothrix orenii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TA9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TA9 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hore_15280 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31909 Halothermothrix orenii])</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ta9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ta9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ta9 RCSB], [http://www.ebi.ac.uk/pdbsum/3ta9 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The beta-glucosidase A gene (bglA) has been cloned from the halothermophilic bacterium Halothermothrix orenii and the recombinant enzyme (BglA; EC 3.2.1.21) was bacterially expressed, purified using metal ion-affinity chromatography and subsequently crystallized. Orthorhombic crystals were obtained that diffracted to a resolution limit of 3.5 A. The crystal structure with two molecules in the asymmetric unit was solved by molecular replacement using a library of known glucosidase structures. Attempts to collect higher resolution diffraction data from crystals grown under different conditions and structure refinement are currently in progress. | |||
Expression, purification and preliminary crystallographic analysis of the recombinant beta-glucosidase (BglA) from the halothermophile Halothermothrix orenii.,Kori LD, Hofmann A, Patel BK Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt 1):111-3. Epub, 2010 Dec 23. PMID:21206038<ref>PMID:21206038</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Beta-glucosidase|Beta-glucosidase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
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[[Category: Beta-glucosidase]] | [[Category: Beta-glucosidase]] | ||
[[Category: Halothermothrix orenii]] | [[Category: Halothermothrix orenii]] | ||
Revision as of 06:06, 5 June 2014
beta-Glucosidase A from the halothermophile H. orenii
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