| pubmed-article:16015376 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16015376 | lifeskim:mentions | umls-concept:C0995888 | lld:lifeskim |
| pubmed-article:16015376 | lifeskim:mentions | umls-concept:C0037473 | lld:lifeskim |
| pubmed-article:16015376 | lifeskim:mentions | umls-concept:C0052088 | lld:lifeskim |
| pubmed-article:16015376 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:16015376 | lifeskim:mentions | umls-concept:C0033727 | lld:lifeskim |
| pubmed-article:16015376 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16015376 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:16015376 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:16015376 | pubmed:dateCreated | 2005-8-3 | lld:pubmed |
| pubmed-article:16015376 | pubmed:abstractText | Na+/H+ antiporters are pH-dependent membrane transport proteins that maintain the homeostasis of H+ and Na+ in living cells. MjNhaP1 from Methanococcus jannaschii, a hyperthermophilic archaeon that grows optimally at 85 degrees C, was cloned and expressed in Escherichia coli. Two-dimensional crystals were obtained from purified protein at pH 4. Electron cryomicroscopy yielded an 8 A projection map. Like the related E. coli antiporter NhaA, MjNhaP1 is a dimer, but otherwise the structures of the two antiporters differ significantly. The map of MjNhaP1 shows elongated densities in the centre of the dimer and a cluster of density peaks on either side of the dimer core, indicative of a bundle of 4-6 membrane-spanning helices. The effect of pH on the structure of MjNhaP1 was studied in situ. A major change in density distribution within the helix bundle, and an approximately 2 A shift in the position of the helix bundle relative to the dimer core occurred at pH 6 and above. The two conformations at low and high pH most likely represent the closed and open states of the antiporter. | lld:pubmed |
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| pubmed-article:16015376 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16015376 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16015376 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16015376 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16015376 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:16015376 | pubmed:author | pubmed-author:KühlbrandtWer... | lld:pubmed |
| pubmed-article:16015376 | pubmed:author | pubmed-author:VinothkumarKu... | lld:pubmed |
| pubmed-article:16015376 | pubmed:author | pubmed-author:SmitsSander... | lld:pubmed |
| pubmed-article:16015376 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16015376 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:16015376 | pubmed:volume | 24 | lld:pubmed |
| pubmed-article:16015376 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16015376 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16015376 | pubmed:pagination | 2720-9 | lld:pubmed |
| pubmed-article:16015376 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:16015376 | pubmed:meshHeading | pubmed-meshheading:16015376... | lld:pubmed |
| pubmed-article:16015376 | pubmed:meshHeading | pubmed-meshheading:16015376... | lld:pubmed |
| pubmed-article:16015376 | pubmed:meshHeading | pubmed-meshheading:16015376... | lld:pubmed |
| pubmed-article:16015376 | pubmed:meshHeading | pubmed-meshheading:16015376... | lld:pubmed |
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| pubmed-article:16015376 | pubmed:meshHeading | pubmed-meshheading:16015376... | lld:pubmed |
| pubmed-article:16015376 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16015376 | pubmed:articleTitle | pH-induced structural change in a sodium/proton antiporter from Methanococcus jannaschii. | lld:pubmed |
| pubmed-article:16015376 | pubmed:affiliation | Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany. | lld:pubmed |
| pubmed-article:16015376 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16015376 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:16015376 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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