Source:http://linkedlifedata.com/resource/pubmed/id/10666592
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 2
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pubmed:dateCreated |
2000-4-5
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pubmed:databankReference | |
pubmed:abstractText |
The structure of xylose isomerase (XyI) from Streptomyces diastaticus No. 7 strain M1033 (SDXyI) has been refined at 1.85 A resolution to conventional and free R factors of 0.166 and 0.219, respectively. SDXyI was crystallized in space group P2(1)2(1)2, with unit-cell parameters a = 87.976, b = 98.836, c = 93.927 A. One dimer of the tetrametric molecule is found in each asymmetric unit. Each monomer consists of two domains: a large N-terminal domain (residues 1-320), containing a parallel eight-stranded alpha/beta barrel, and a small C-terminal loop (residues 321-387), containing five helices linked by random coil. The four monomers are essentially identical in the tetramer, possessing non-crystallographic 222 symmetry with one twofold axis essentially coincident with the crystallographic twofold axis in the space group P2(1)2(1)2, which may explain why the diffraction pattern has strong pseudo-I222 symmetry even at medium resolution. The crystal structures of XyIs from different bacterial strains, especially from Streptomyces, are similar. The alpha2 helix of the alpha/beta barrel has a different position in the structures of different XyIs. The conformation of C-terminal fragment 357-364 in the SDXyI structure has a small number of differences to that of other XyIs. Two Co(2+) ions rather than Mg(2+) ions exist in the active site of the SDXyI structure; SDXyI seems to prefer to bind Co(2+) ions rather than Mg(2+) ions.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aldose-Ketose Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cobalt,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions,
http://linkedlifedata.com/resource/pubmed/chemical/Water,
http://linkedlifedata.com/resource/pubmed/chemical/xylose isomerase
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
56
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
129-36
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10666592-Aldose-Ketose Isomerases,
pubmed-meshheading:10666592-Amino Acid Sequence,
pubmed-meshheading:10666592-Bacterial Proteins,
pubmed-meshheading:10666592-Binding Sites,
pubmed-meshheading:10666592-Cobalt,
pubmed-meshheading:10666592-Crystallography, X-Ray,
pubmed-meshheading:10666592-Dimerization,
pubmed-meshheading:10666592-Magnesium,
pubmed-meshheading:10666592-Manganese,
pubmed-meshheading:10666592-Molecular Sequence Data,
pubmed-meshheading:10666592-Sequence Homology, Amino Acid,
pubmed-meshheading:10666592-Solutions,
pubmed-meshheading:10666592-Streptomyces,
pubmed-meshheading:10666592-Structure-Activity Relationship,
pubmed-meshheading:10666592-Water
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pubmed:year |
2000
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pubmed:articleTitle |
Structure of xylose isomerase from Streptomyces diastaticus no. 7 strain M1033 at 1.85 A resolution.
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pubmed:affiliation |
Department of Molecular Biology, School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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