| pubmed-article:18819925 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18819925 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
| pubmed-article:18819925 | lifeskim:mentions | umls-concept:C0002520 | lld:lifeskim |
| pubmed-article:18819925 | lifeskim:mentions | umls-concept:C0032433 | lld:lifeskim |
| pubmed-article:18819925 | lifeskim:mentions | umls-concept:C0596902 | lld:lifeskim |
| pubmed-article:18819925 | lifeskim:mentions | umls-concept:C0033363 | lld:lifeskim |
| pubmed-article:18819925 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:18819925 | lifeskim:mentions | umls-concept:C1883220 | lld:lifeskim |
| pubmed-article:18819925 | pubmed:issue | 48 | lld:pubmed |
| pubmed-article:18819925 | pubmed:dateCreated | 2008-11-25 | lld:pubmed |
| pubmed-article:18819925 | pubmed:abstractText | The L-arginine/agmatine antiporter AdiC is a key component of the arginine-dependent extreme acid resistance system of Escherichia coli. Phylogenetic analysis indicated that AdiC belongs to the amino acid/polyamine/organocation (APC) transporter superfamily having sequence identities of 15-17% to eukaryotic and human APC transporters. For functional and structural characterization, we cloned, overexpressed, and purified wild-type AdiC and the point mutant AdiC-W293L, which is unable to bind and consequently transport L-arginine. Purified detergent-solubilized AdiC particles were dimeric. Reconstitution experiments yielded two-dimensional crystals of AdiC-W293L diffracting beyond 6 angstroms resolution from which we determined the projection structure at 6.5 angstroms resolution. The projection map showed 10-12 density peaks per monomer and suggested mainly tilted helices with the exception of one distinct perpendicular membrane spanning alpha-helix. Comparison of AdiC-W293L with the projection map of the oxalate/formate antiporter from Oxalobacter formigenes, a member from the major facilitator superfamily, indicated different structures. Thus, two-dimensional crystals of AdiC-W293L yielded the first detailed view of a transport protein from the APC superfamily at sub-nanometer resolution. | lld:pubmed |
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| pubmed-article:18819925 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18819925 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18819925 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18819925 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:18819925 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:18819925 | pubmed:author | pubmed-author:EngelAndreasA | lld:pubmed |
| pubmed-article:18819925 | pubmed:author | pubmed-author:FotiadisDimit... | lld:pubmed |
| pubmed-article:18819925 | pubmed:author | pubmed-author:ChamiMohamedM | lld:pubmed |
| pubmed-article:18819925 | pubmed:author | pubmed-author:CasagrandeFab... | lld:pubmed |
| pubmed-article:18819925 | pubmed:author | pubmed-author:PalacinManuel... | lld:pubmed |
| pubmed-article:18819925 | pubmed:author | pubmed-author:TorrentsDavid... | lld:pubmed |
| pubmed-article:18819925 | pubmed:author | pubmed-author:ValenciaEvaE | lld:pubmed |
| pubmed-article:18819925 | pubmed:author | pubmed-author:SchenkAndreas... | lld:pubmed |
| pubmed-article:18819925 | pubmed:author | pubmed-author:RateraMerceM | lld:pubmed |
| pubmed-article:18819925 | pubmed:author | pubmed-author:LopezJesus... | lld:pubmed |
| pubmed-article:18819925 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18819925 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:18819925 | pubmed:volume | 283 | lld:pubmed |
| pubmed-article:18819925 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18819925 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18819925 | pubmed:pagination | 33240-8 | lld:pubmed |
| pubmed-article:18819925 | pubmed:dateRevised | 2010-9-21 | lld:pubmed |
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| pubmed-article:18819925 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18819925 | pubmed:articleTitle | Projection structure of a member of the amino acid/polyamine/organocation transporter superfamily. | lld:pubmed |
| pubmed-article:18819925 | pubmed:affiliation | M. E. Müller Institute for Structural Biology, Biozentrum of the University of Basel, CH-4056 Basel, Switzerland. | lld:pubmed |
| pubmed-article:18819925 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18819925 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:948628 | entrezgene:pubmed | pubmed-article:18819925 | lld:entrezgene |
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