Crystallization of selenomethionyl exo-beta-1,3-galactanase from the basidiomycete Phanerochaete chrysosporium.
Identifieur interne : 000643 ( Main/Exploration ); précédent : 000642; suivant : 000644Crystallization of selenomethionyl exo-beta-1,3-galactanase from the basidiomycete Phanerochaete chrysosporium.
Auteurs : Takuya Ishida [Japon] ; Zui Fujimoto ; Hitomi Ichinose ; Kiyohiko Igarashi ; Satoshi Kaneko ; Masahiro SamejimaSource :
- Acta crystallographica. Section F, Structural biology and crystallization communications [ 1744-3091 ] ; 2009.
Descripteurs français
- KwdFr :
- Clonage moléculaire (MeSH), Conformation des protéines (MeSH), Cristallisation (MeSH), Cristallographie aux rayons X (MeSH), Glycosidases (composition chimique), Glycosidases (génétique), Phanerochaete (enzymologie), Phanerochaete (génétique), Pichia (génétique), Pichia (métabolisme), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique).
- MESH :
- composition chimique : Glycosidases, Protéines recombinantes.
- enzymologie : Phanerochaete.
- génétique : Glycosidases, Phanerochaete, Pichia, Protéines recombinantes.
- métabolisme : Pichia.
- Clonage moléculaire, Conformation des protéines, Cristallisation, Cristallographie aux rayons X.
English descriptors
- KwdEn :
- Cloning, Molecular (MeSH), Crystallization (MeSH), Crystallography, X-Ray (MeSH), Glycoside Hydrolases (chemistry), Glycoside Hydrolases (genetics), Phanerochaete (enzymology), Phanerochaete (genetics), Pichia (genetics), Pichia (metabolism), Protein Conformation (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics).
- MESH :
- chemical , chemistry : Glycoside Hydrolases, Recombinant Proteins.
- chemical , genetics : Glycoside Hydrolases, Recombinant Proteins.
- enzymology : Phanerochaete.
- genetics : Phanerochaete, Pichia.
- metabolism : Pichia.
- Cloning, Molecular, Crystallization, Crystallography, X-Ray, Protein Conformation.
Abstract
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.
DOI: 10.1107/S1744309109043395
PubMed: 20054127
PubMed Central: PMC2802879
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<front><div type="abstract" xml:lang="en">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.</div>
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<Abstract><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.</AbstractText>
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