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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 2
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pubmed:dateCreated |
2006-3-2
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pubmed:abstractText |
EstE1, a new thermostable esterase, was isolated by functional screening of a metagenomic DNA library from thermal environment samples. This enzyme showed activity towards short-chain acyl derivatives of length C4-C6 at a temperature of 303-363 K and displayed a high thermostability above 353 K. EstE1 has 64 and 57% amino-acid sequence similarity to est(pc)-encoded carboxylesterase from Pyrobaculum calidifontis and AFEST from Archaeoglobus fulgidus, respectively. The recombinant protein with a histidine tag at the C-terminus was overexpressed in Escherichia coli strain BL21(DE3) and then purified by affinity chromatography. The protein was crystallized at 290 K by the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 2.3 A resolution from an EstE1 crystal; the crystal belongs to space group P4(1)2(1)2, with unit-cell parameters a = b = 73.71, c = 234.23 A. Assuming the presence of four molecules in the asymmetric unit, the Matthews coefficient VM is calculated to be 2.2 A3 Da(-1) and the solvent content is 44.1%.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511287-10201402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511287-10493927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511287-10547694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511287-10607665,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511287-10620337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511287-11061974,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511287-11846563,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511287-11867217,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511287-12147492,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511287-12482512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511287-12676497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511287-1409539
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1744-3091
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
62
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
145-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16511287-Archaeal Proteins,
pubmed-meshheading:16511287-Archaeoglobus fulgidus,
pubmed-meshheading:16511287-Carboxylesterase,
pubmed-meshheading:16511287-Cloning, Molecular,
pubmed-meshheading:16511287-Crystallization,
pubmed-meshheading:16511287-Crystallography, X-Ray,
pubmed-meshheading:16511287-Enzyme Stability,
pubmed-meshheading:16511287-Genomic Library,
pubmed-meshheading:16511287-Pyrobaculum,
pubmed-meshheading:16511287-Recombinant Proteins,
pubmed-meshheading:16511287-Temperature
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pubmed:year |
2006
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pubmed:articleTitle |
Crystallization and preliminary X-ray crystallographic analysis of EstE1, a new and thermostable esterase cloned from a metagenomic library.
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pubmed:affiliation |
Department of Biology, Yonsei University, Seoul 120-749, South Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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