Source:http://linkedlifedata.com/resource/pubmed/id/17183164
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 1
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pubmed:dateCreated |
2006-12-21
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pubmed:abstractText |
6-Pyruvoyl tetrahydrobiopterin synthase (PTPS) catalyses the conversion of dihydroneopterin triphosphate to 6-pyruvoyl tetrahydropterin, the second of the three enzymatic steps in the synthesis of tetrahydrobiopterin from GTP. PH0634, a 13.51 kDa archaeal PTPS homologue from Pyrococcus horikoshii OT3, was overexpressed as native and selenomethionine-substituted protein and the purified protein was crystallized by the oil-microbatch method at 295 K. X-ray diffraction data were collected to 2.1 A resolution from the native crystal using synchrotron radiation at 100 K. The crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 35.83, b = 95.71, c = 105.65 A. Threefold noncrystallographic symmetry was identified from self-rotation calculations. Assuming the presence of a trimer in the asymmetric unit, the solvent content is 45% (V(M) = 2.24 A3 Da(-1)). The selenomethionine-substituted crystal is isomorphous to the native crystal and diffracts X-rays to 2.9 A.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17183164-10024455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17183164-10089316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17183164-10727395,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17183164-12099018,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17183164-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17183164-2184035,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17183164-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17183164-5700707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17183164-7563095,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17183164-8137809
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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 |
Jan
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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 |
63
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:17183164-Archaeal Proteins,
pubmed-meshheading:17183164-Crystallization,
pubmed-meshheading:17183164-Crystallography, X-Ray,
pubmed-meshheading:17183164-Phosphorus-Oxygen Lyases,
pubmed-meshheading:17183164-Pyrococcus horikoshii,
pubmed-meshheading:17183164-Structural Homology, Protein
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pubmed:year |
2007
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pubmed:articleTitle |
Purification, crystallization and preliminary crystallographic analysis of archaeal 6-pyruvoyl tetrahydrobiopterin synthase homologue PH0634 from Pyrococcus horikoshii OT3.
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pubmed:affiliation |
Advanced Protein Crystallography Research Group, RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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