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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1984-5-4
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pubmed:abstractText |
The binding to glycogen phosphorylase b of glucose 6-phosphate and inorganic phosphate (respectively allosteric inhibitor and substrate/activator of the enzyme) were studied in the crystal at 0.3 nm (3A) resolution. Glucose 6-phosphate binds in the alpha-configuration at a site that is close to the AMP allosteric effector site at the subunit-subunit interface and promotes several conformational changes. The phosphate-binding site of the enzyme for glucose 6-phosphate involves contacts to two cationic residues, Arg-309 and Lys-247. This site is also occupied in the inorganic-phosphate-binding studies and is therefore identified as a high-affinity phosphate-binding site. It is distinct from the weaker phosphate-binding site of the enzyme for AMP, which is 0.27 nm (2.7A) away. The glucose moiety of glucose 6-phosphate and the adenosine moiety of AMP do not overlap. The results provide a structural explanation for the kinetic observations that glucose 6-phosphate inhibition of AMP activation of phosphorylase b is partially competitive and highly co-operative. The results suggest that the transmission of allosteric conformational changes involves an increase in affinity at phosphate-binding sites and relative movements of alpha-helices. In order to study glucose 6-phosphate and phosphate binding it was necessary to cross-link the crystals. The use of dimethyl malondi-imidate as a new cross-linking reagent in protein crystallography is discussed.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-1009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-119868,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-1236149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-14104598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-14235520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-14343300,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-16386049,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-173552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-224918,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-226120,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-270711,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-326146,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-39173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-4301224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-4318155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-4382801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-4449138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-4741557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-4819639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-4853384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-5432802,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-5551392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-5696505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-5702046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-5723454,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-641070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-6415289,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-6551233,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-6768356,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-6776286,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-6781495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-6788104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-6832361,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-6966688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-721833,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-7306067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-875032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-949983,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6424657-992029
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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 |
Feb
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
218
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
45-60
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:6424657-Adenosine Monophosphate,
pubmed-meshheading:6424657-Allosteric Regulation,
pubmed-meshheading:6424657-Allosteric Site,
pubmed-meshheading:6424657-Binding Sites,
pubmed-meshheading:6424657-Crystallography,
pubmed-meshheading:6424657-Glucose-6-Phosphate,
pubmed-meshheading:6424657-Glucosephosphates,
pubmed-meshheading:6424657-Imidoesters,
pubmed-meshheading:6424657-Models, Molecular,
pubmed-meshheading:6424657-Phosphates,
pubmed-meshheading:6424657-Phosphorylase b,
pubmed-meshheading:6424657-Phosphorylases,
pubmed-meshheading:6424657-Protein Conformation
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pubmed:year |
1984
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pubmed:articleTitle |
Allosteric interactions of glycogen phosphorylase b. A crystallographic study of glucose 6-phosphate and inorganic phosphate binding to di-imidate-cross-linked phosphorylase b.
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pubmed:publicationType |
Journal Article
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