pubmed-article:10924108 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10924108 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
pubmed-article:10924108 | lifeskim:mentions | umls-concept:C0007590 | lld:lifeskim |
pubmed-article:10924108 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
pubmed-article:10924108 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
pubmed-article:10924108 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:10924108 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
pubmed-article:10924108 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
pubmed-article:10924108 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
pubmed-article:10924108 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
pubmed-article:10924108 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
pubmed-article:10924108 | pubmed:issue | 31 | lld:pubmed |
pubmed-article:10924108 | pubmed:dateCreated | 2000-9-7 | lld:pubmed |
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pubmed-article:10924108 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10924108 | pubmed:abstractText | ZipA, an essential component of cell division in Escherichia coli, interacts with the FtsZ protein at the midcell in one of the initial steps of septum formation. The high-resolution solution structure of the 144-residue C-terminal domain of E. coli ZipA (ZipA(185)(-)(328)) has been determined by multidimensional heteronuclear NMR. A total of 30 structures were calculated by means of hybrid distance geometry-simulated annealing using a total of 2758 experimental NMR restraints. The atomic root means square distribution about the mean coordinate positions for residues 6-142 for the 30 structures is 0.37 +/- 0.04 A for the backbone atoms, 0. 78 +/- 0.05 A for all atoms, and 0.45 +/- 0.04 A for all atoms excluding disordered side chains. The NMR solution structure of ZipA(185)(-)(328) is composed of three alpha-helices and a beta-sheet consisting of six antiparallel beta-strands where the alpha-helices and the beta-sheet form surfaces directly opposite each other. A C-terminal peptide from FtsZ has been shown to bind ZipA(185)(-)(328) in a hydrophobic channel formed by the beta-sheet providing insight into the ZipA-FtsZ interaction. An unexpected similarity between the ZipA(185)(-)(328) fold and the split beta-alpha-beta fold observed in many RNA binding proteins may further our understanding of the critical ZipA-FtsZ interaction. | lld:pubmed |
pubmed-article:10924108 | pubmed:language | eng | lld:pubmed |
pubmed-article:10924108 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10924108 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10924108 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10924108 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10924108 | pubmed:month | Aug | lld:pubmed |
pubmed-article:10924108 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:10924108 | pubmed:author | pubmed-author:PowersRR | lld:pubmed |
pubmed-article:10924108 | pubmed:author | pubmed-author:MoyF JFJ | lld:pubmed |
pubmed-article:10924108 | pubmed:author | pubmed-author:MosyakLL | lld:pubmed |
pubmed-article:10924108 | pubmed:author | pubmed-author:GlasfeldEE | lld:pubmed |
pubmed-article:10924108 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10924108 | pubmed:day | 8 | lld:pubmed |
pubmed-article:10924108 | pubmed:volume | 39 | lld:pubmed |
pubmed-article:10924108 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10924108 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10924108 | pubmed:pagination | 9146-56 | lld:pubmed |
pubmed-article:10924108 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
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pubmed-article:10924108 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10924108 | pubmed:articleTitle | Solution structure of ZipA, a crucial component of Escherichia coli cell division. | lld:pubmed |
pubmed-article:10924108 | pubmed:affiliation | Department of Biological Chemistry, Wyeth Research, Cambridge, Massachusetts 02140, USA. | lld:pubmed |
pubmed-article:10924108 | pubmed:publicationType | Journal Article | lld:pubmed |
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