| pubmed-article:19761218 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19761218 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:19761218 | lifeskim:mentions | umls-concept:C0017932 | lld:lifeskim |
| pubmed-article:19761218 | lifeskim:mentions | umls-concept:C2611259 | lld:lifeskim |
| pubmed-article:19761218 | pubmed:issue | 42 | lld:pubmed |
| pubmed-article:19761218 | pubmed:dateCreated | 2009-10-20 | lld:pubmed |
| pubmed-article:19761218 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19761218 | pubmed:abstractText | Glycogen/starch synthase elongates glucan chains and is the key enzyme in the synthesis of glycogen in bacteria and starch in plants. Cocrystallization of Escherichia coli wild-type glycogen synthase (GS) with substrate ADPGlc and the glucan acceptor mimic HEPPSO produced a closed form of GS and suggests that domain-domain closure accompanies glycogen synthesis. Cocrystallization of the inactive GS mutant E377A with substrate ADPGlc and oligosaccharide results in the first oligosaccharide-bound glycogen synthase structure. Four bound oligosaccharides are observed, one in the interdomain cleft (G6a) and three on the N-terminal domain surface (G6b, G6c, and G6d). Extending from the center of the enzyme to the interdomain cleft opening, G6a mostly interacts with the highly conserved N-terminal domain residues lining the cleft of GS. The surface-bound oligosaccharides G6c and G6d have less interaction with enzyme and exhibit a more curled, helixlike structural arrangement. The observation that oligosaccharides bind only to the N-terminal domain of GS suggests that glycogen in vivo probably binds to only one side of the enzyme to ensure unencumbered interdomain movement, which is required for efficient, continuous glucan-chain synthesis. | lld:pubmed |
| pubmed-article:19761218 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19761218 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19761218 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19761218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19761218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19761218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19761218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19761218 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19761218 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:19761218 | pubmed:issn | 1520-4995 | lld:pubmed |
| pubmed-article:19761218 | pubmed:author | pubmed-author:DeysSS | lld:pubmed |
| pubmed-article:19761218 | pubmed:author | pubmed-author:GeigerJames... | lld:pubmed |
| pubmed-article:19761218 | pubmed:author | pubmed-author:PreissJackJ | lld:pubmed |
| pubmed-article:19761218 | pubmed:author | pubmed-author:YepAlejandraA | lld:pubmed |
| pubmed-article:19761218 | pubmed:author | pubmed-author:FangShengS | lld:pubmed |
| pubmed-article:19761218 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19761218 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:19761218 | pubmed:volume | 48 | lld:pubmed |
| pubmed-article:19761218 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19761218 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19761218 | pubmed:pagination | 10089-97 | lld:pubmed |
| pubmed-article:19761218 | pubmed:meshHeading | pubmed-meshheading:19761218... | lld:pubmed |
| pubmed-article:19761218 | pubmed:meshHeading | pubmed-meshheading:19761218... | lld:pubmed |
| pubmed-article:19761218 | pubmed:meshHeading | pubmed-meshheading:19761218... | lld:pubmed |
| pubmed-article:19761218 | pubmed:meshHeading | pubmed-meshheading:19761218... | lld:pubmed |
| pubmed-article:19761218 | pubmed:meshHeading | pubmed-meshheading:19761218... | lld:pubmed |
| pubmed-article:19761218 | pubmed:meshHeading | pubmed-meshheading:19761218... | lld:pubmed |
| pubmed-article:19761218 | pubmed:meshHeading | pubmed-meshheading:19761218... | lld:pubmed |
| pubmed-article:19761218 | pubmed:meshHeading | pubmed-meshheading:19761218... | lld:pubmed |
| pubmed-article:19761218 | pubmed:meshHeading | pubmed-meshheading:19761218... | lld:pubmed |
| pubmed-article:19761218 | pubmed:meshHeading | pubmed-meshheading:19761218... | lld:pubmed |
| pubmed-article:19761218 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19761218 | pubmed:articleTitle | Oligosaccharide binding in Escherichia coli glycogen synthase. | lld:pubmed |
| pubmed-article:19761218 | pubmed:affiliation | Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, USA. | lld:pubmed |
| pubmed-article:19761218 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19761218 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:19761218 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:947932 | entrezgene:pubmed | pubmed-article:19761218 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19761218 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19761218 | lld:pubmed |
