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rdf:type |
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lifeskim:mentions |
umls-concept:C0010423,
umls-concept:C0014834,
umls-concept:C0021237,
umls-concept:C0037633,
umls-concept:C0243071,
umls-concept:C0377355,
umls-concept:C0439855,
umls-concept:C0678594,
umls-concept:C1382100,
umls-concept:C1514562,
umls-concept:C1710236,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2699488
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pubmed:issue |
3
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pubmed:dateCreated |
1990-5-25
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pubmed:abstractText |
The recombinant synthase domain of the bifunctional enzyme N-(5'-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli has been crystallized, and the structure has been solved at 4 A resolution. Two closely related crystal forms grown from ammonium sulphate diffract to 2 A resolution. One form (space group R32, a = 163 A, alpha = 29.5 degrees) contains the unliganded synthase domain; the second crystal form (space group P6(3)22, a = 144 A, c = 158 A) is co-crystallized with the substrate analogue N-(5'-phosphoribit-1-yl)anthranilate. The structure of the synthase-inhibitor complex has been solved by the molecular replacement method. This achievement represents the first successful use of a (beta alpha)8-barrel monomer as a trial model. The recombinant synthase domain associates as a trimer in the crystal, the molecules being related by a pseudo-crystallographic triad. The interface contacts between the three domains are mediated by those residues that are also involved in the domain interface of the bifunctional enzyme. This system provides a model for an interface which is used in both intermolecular and intramolecular domain contacts.
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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 |
Jan
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pubmed:issn |
0269-2139
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
173-80
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:2184433-Aldose-Ketose Isomerases,
pubmed-meshheading:2184433-Anthranilic Acids,
pubmed-meshheading:2184433-Carbohydrate Epimerases,
pubmed-meshheading:2184433-Carboxy-Lyases,
pubmed-meshheading:2184433-Crystallization,
pubmed-meshheading:2184433-Dithionitrobenzoic Acid,
pubmed-meshheading:2184433-Escherichia coli,
pubmed-meshheading:2184433-Indole-3-Glycerol-Phosphate Synthase,
pubmed-meshheading:2184433-Macromolecular Substances,
pubmed-meshheading:2184433-Molecular Structure,
pubmed-meshheading:2184433-Recombinant Proteins,
pubmed-meshheading:2184433-Ribosemonophosphates,
pubmed-meshheading:2184433-X-Ray Diffraction
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pubmed:year |
1990
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pubmed:articleTitle |
Crystallization and structure solution at 4 A resolution of the recombinant synthase domain of N-(5'-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli complexed to a substrate analogue.
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pubmed:affiliation |
Department of Structural Biology, University of Basel, Switzerland.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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