| pubmed-article:9000079 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9000079 | lifeskim:mentions | umls-concept:C0031656 | lld:lifeskim |
| pubmed-article:9000079 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:9000079 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:9000079 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:9000079 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:9000079 | pubmed:issue | 6613 | lld:pubmed |
| pubmed-article:9000079 | pubmed:dateCreated | 1997-2-6 | lld:pubmed |
| pubmed-article:9000079 | pubmed:abstractText | Phosphoglycerate kinase (PGK), a key enzyme in glycolysis, catalyses the transfer of a phosphoryl-group from 1,3-bisphosphoglycerate to ADP to form 3-phosphoglycerate and ATP. Despite extensive kinetic and structural investigations over more than two decades, the conformation assumed by this enzyme during catalysis remained unknown. Here we present the 2.8 A crystal structure of a ternary complex of PGK from Trypanosoma brucei, the causative agent of sleeping sickness. This structure determination relied on a procedure in which fragments containing less than 10% of the scattering mass were successively positioned in the unit cell to obtain phases. The PGK ternary complex exhibits a dramatic closing of the large cleft between the two domains seen in all previous studies, thereby bringing the two ligands, 3-phosphoglycerate and ADP into close proximity. Our results demonstrate that PGK is a hinge-bending enzyme, reveal a novel mechanism in which substrate-induced effects combine synergistically to induce major conformational changes and, to our knowledge, afford the first observation of the PGK active site in a catalytic conformation. | lld:pubmed |
| pubmed-article:9000079 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9000079 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9000079 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9000079 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9000079 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9000079 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9000079 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9000079 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9000079 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9000079 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9000079 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:9000079 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:9000079 | pubmed:author | pubmed-author:MichelsP APA | lld:pubmed |
| pubmed-article:9000079 | pubmed:author | pubmed-author:HolW GWG | lld:pubmed |
| pubmed-article:9000079 | pubmed:author | pubmed-author:BernsteinB... | lld:pubmed |
| pubmed-article:9000079 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9000079 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:9000079 | pubmed:volume | 385 | lld:pubmed |
| pubmed-article:9000079 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9000079 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9000079 | pubmed:pagination | 275-8 | lld:pubmed |
| pubmed-article:9000079 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9000079 | pubmed:meshHeading | pubmed-meshheading:9000079-... | lld:pubmed |
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| pubmed-article:9000079 | pubmed:meshHeading | pubmed-meshheading:9000079-... | lld:pubmed |
| pubmed-article:9000079 | pubmed:meshHeading | pubmed-meshheading:9000079-... | lld:pubmed |
| pubmed-article:9000079 | pubmed:meshHeading | pubmed-meshheading:9000079-... | lld:pubmed |
| pubmed-article:9000079 | pubmed:meshHeading | pubmed-meshheading:9000079-... | lld:pubmed |
| pubmed-article:9000079 | pubmed:meshHeading | pubmed-meshheading:9000079-... | lld:pubmed |
| pubmed-article:9000079 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9000079 | pubmed:articleTitle | Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation. | lld:pubmed |
| pubmed-article:9000079 | pubmed:affiliation | Department of Biochemistry, Biomolecular Structure Center, University of Washington, Seattle 98195, USA. | lld:pubmed |
| pubmed-article:9000079 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9000079 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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