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rdf:type |
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lifeskim:mentions |
umls-concept:C0014442,
umls-concept:C0014834,
umls-concept:C0019602,
umls-concept:C0031642,
umls-concept:C0031727,
umls-concept:C0205681,
umls-concept:C0242209,
umls-concept:C1442792,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
3
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pubmed:dateCreated |
1998-5-14
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pubmed:abstractText |
The phosphorylated form of the N-terminal domain of enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli has been investigated by one-bond and long-range 1H-15N correlation spectroscopy. The active site His 189 is phosphorylated at the Nepsilon2 position and has a pKa of 7.3, which is one pH unit higher than that of unphosphorylated His 189. Because the neutral form of unphosphorylated His 189 is in the Ndelta1-H tautomer, and its Nepsilon2 atom is solvent inaccessible and accepts a hydrogen bond from the hydroxyl group of Thr 168, both protonation and phosphorylation of His 189 must be accompanied by a change in the side-chain conformation of His 189, specifically from a chi(2) angle in the g+ conformer in the unphosphorylated state to the g- conformer in the phosphorylated state.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9541412-1655788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9541412-1821787,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9541412-6754730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9541412-7712285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9541412-7853396,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9541412-8031118,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9541412-8518729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9541412-8520220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9541412-8555180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9541412-8692938,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9541412-9054557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9541412-9109646,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9541412-925263
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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 |
Mar
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
789-93
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9541412-Bacterial Proteins,
pubmed-meshheading:9541412-Binding Sites,
pubmed-meshheading:9541412-Escherichia coli,
pubmed-meshheading:9541412-Histidine,
pubmed-meshheading:9541412-Models, Molecular,
pubmed-meshheading:9541412-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:9541412-Phosphoenolpyruvate Sugar Phosphotransferase System,
pubmed-meshheading:9541412-Phosphorylation,
pubmed-meshheading:9541412-Protein Structure, Tertiary
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pubmed:year |
1998
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pubmed:articleTitle |
Tautomeric state and pKa of the phosphorylated active site histidine in the N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system.
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pubmed:affiliation |
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA.
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pubmed:publicationType |
Journal Article
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