Source:http://linkedlifedata.com/resource/pubmed/id/20054127
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 12
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pubmed:dateCreated |
2010-1-7
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pubmed:abstractText |
Exo-beta-1,3-galactanase from Phanerochaete chrysosporium (Pc1,3Gal43A) consists of a glycoside hydrolase family 43 catalytic domain and a substrate-binding domain that belongs to carbohydrate-binding module family 35. It catalyzes the hydrolysis of beta-1,3-galactan, which is the backbone of the arabinogalactan proteins; the C-terminal carbohydrate-binding module family 35 domain increases the local concentration of the enzyme around beta-1,3-galactan by its high affinity for the substrate. To enable phase determination using the multiwavelength anomalous dispersion method, selenomethionyl Pc1,3Gal43A was crystallized at 298 K using the hanging-drop vapour-diffusion method. The presence of selenium in the crystals was confirmed from the X-ray absorption spectrum. The crystals belonged to space group P2(1) and diffracted to 1.8 A resolution.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1744-3091
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
65
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1274-6
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pubmed:meshHeading |
pubmed-meshheading:20054127-Cloning, Molecular,
pubmed-meshheading:20054127-Crystallization,
pubmed-meshheading:20054127-Crystallography, X-Ray,
pubmed-meshheading:20054127-Glycoside Hydrolases,
pubmed-meshheading:20054127-Phanerochaete,
pubmed-meshheading:20054127-Pichia,
pubmed-meshheading:20054127-Protein Conformation,
pubmed-meshheading:20054127-Recombinant Proteins
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pubmed:year |
2009
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pubmed:articleTitle |
Crystallization of selenomethionyl exo-beta-1,3-galactanase from the basidiomycete Phanerochaete chrysosporium.
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pubmed:affiliation |
Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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