| pubmed-article:8831790 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8831790 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:8831790 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:8831790 | lifeskim:mentions | umls-concept:C1619833 | lld:lifeskim |
| pubmed-article:8831790 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8831790 | pubmed:dateCreated | 1996-11-7 | lld:pubmed |
| pubmed-article:8831790 | pubmed:abstractText | The crystal structure of the glutamine-binding protein (GlnBP) from Escherichia coli in a ligand-free "open" conformational state has been determined by isomorphous replacement methods and refined to an R-value of 21.4% at 2.3 A resolution. There are two molecules in the asymmetric unit, related by pseudo 4-fold screw symmetry. The refined model consists of 3587 non-hydrogen atoms from 440 residues (two monomers), and 159 water molecules. The structure has root-mean-square deviations of 0.013 A from "ideal" bond lengths and 1.5 degrees from "ideal" bond angles. The GlnBP molecule has overall dimensions of approximately 60 A x 40 A x 35 A and is made up of two domains (termed large and small), which exhibit a similar supersecondary structure, linked by two antiparallel beta-strands. The small domain contains three alpha-helices and four parallel and one antiparallel beta-strands. The large domain is similar to the small domain but contains two additional alpha-helices and three more short antiparallel beta-strands. A comparison of the secondary structural motifs of GlnBP with those of other periplasmic binding proteins is discussed. A model of the "closed form" GlnBP-Gln complex has been proposed based on the crystal structures of the histidine-binding protein-His complex and "open form" GlnBP. This model has been successfully used as a search model in the crystal structure determination of the "closed form" GlnBP-Gln complex by molecular replacement methods. The model agrees remarkably well with the crystal structure of the Gln-GlnBP complex with root-mean-square deviation of 1.29 A. Our study shows that, at least in our case, it is possible to predict one conformational state of a periplasmic binding protein from another conformational state of the protein. The glutamine-binding pockets of the model and the crystal structure are compared and the modeling technique is described. | lld:pubmed |
| pubmed-article:8831790 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8831790 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8831790 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8831790 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8831790 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8831790 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8831790 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8831790 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8831790 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:8831790 | pubmed:author | pubmed-author:WangB CBC | lld:pubmed |
| pubmed-article:8831790 | pubmed:author | pubmed-author:RoseJJ | lld:pubmed |
| pubmed-article:8831790 | pubmed:author | pubmed-author:SunY JYJ | lld:pubmed |
| pubmed-article:8831790 | pubmed:author | pubmed-author:HsiaoC DCD | lld:pubmed |
| pubmed-article:8831790 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8831790 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:8831790 | pubmed:volume | 262 | lld:pubmed |
| pubmed-article:8831790 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8831790 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8831790 | pubmed:pagination | 225-42 | lld:pubmed |
| pubmed-article:8831790 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8831790 | pubmed:meshHeading | pubmed-meshheading:8831790-... | lld:pubmed |
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| pubmed-article:8831790 | pubmed:meshHeading | pubmed-meshheading:8831790-... | lld:pubmed |
| pubmed-article:8831790 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8831790 | pubmed:articleTitle | The crystal structure of glutamine-binding protein from Escherichia coli. | lld:pubmed |
| pubmed-article:8831790 | pubmed:affiliation | Department of Crystallography, University of Pittsburgh, PA 15260, USA. | lld:pubmed |
| pubmed-article:8831790 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8831790 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8831790 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8831790 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:8831790 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:8831790 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:944872 | entrezgene:pubmed | pubmed-article:8831790 | lld:entrezgene |
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