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rdf:type |
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lifeskim:mentions |
umls-concept:C0010423,
umls-concept:C0017262,
umls-concept:C0043309,
umls-concept:C0069147,
umls-concept:C0185117,
umls-concept:C0439611,
umls-concept:C0872384,
umls-concept:C0936012,
umls-concept:C0995888,
umls-concept:C1998793,
umls-concept:C2911684
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pubmed:issue |
Pt 6
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pubmed:dateCreated |
2006-3-2
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pubmed:abstractText |
Methanocaldococcus jannaschii nucleoside kinase (MjNK) is an ATP-dependent non-allosteric phosphotransferase that shows high catalytic activity for guanosine, inosine and cytidine. MjNK is a member of the phosphofructokinase B family, but participates in the biosynthesis of nucleoside monophosphates rather than in glycolysis. MjNK was crystallized as the apoenzyme as well as in complex with an ATP analogue and Mg2+. The latter crystal form was also soaked with fructose-6-phosphate. Synchrotron-radiation data were collected to 1.70 A for the apoenzyme crystals and 1.93 A for the complex crystals. All crystals exhibit orthorhombic symmetry; however, the apoenzyme crystals contain one monomer per asymmetric unit whereas the complex crystals contain a dimer.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-10795681,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-10801355,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-11286887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-11778837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-11797046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-11976749,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-12235162,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-15210349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-1850730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-2185018,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-5700707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-7608978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-8382990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-8688087,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-9519409,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511104-9843365
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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 |
Jun
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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 |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
591-4
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16511104-Adenosine Triphosphate,
pubmed-meshheading:16511104-Apoenzymes,
pubmed-meshheading:16511104-Bacterial Proteins,
pubmed-meshheading:16511104-Cloning, Molecular,
pubmed-meshheading:16511104-Crystallization,
pubmed-meshheading:16511104-Dimerization,
pubmed-meshheading:16511104-Escherichia coli,
pubmed-meshheading:16511104-Euryarchaeota,
pubmed-meshheading:16511104-Fructosephosphates,
pubmed-meshheading:16511104-Magnesium,
pubmed-meshheading:16511104-Phosphofructokinases,
pubmed-meshheading:16511104-Phosphotransferases,
pubmed-meshheading:16511104-Volatilization,
pubmed-meshheading:16511104-X-Ray Diffraction
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pubmed:year |
2005
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pubmed:articleTitle |
Expression, purification, crystallization and preliminary X-ray analysis of a nucleoside kinase from the hyperthermophile Methanocaldococcus jannaschii.
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pubmed:affiliation |
Center for Structural Biochemistry, Department of Biosciences at Novum, Karolinska Institute, S-141 57 Huddinge, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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