| pubmed-article:18203838 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18203838 | lifeskim:mentions | umls-concept:C0439849 | lld:lifeskim |
| pubmed-article:18203838 | lifeskim:mentions | umls-concept:C0205107 | lld:lifeskim |
| pubmed-article:18203838 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:18203838 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:18203838 | lifeskim:mentions | umls-concept:C1423607 | lld:lifeskim |
| pubmed-article:18203838 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:18203838 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:18203838 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:18203838 | lifeskim:mentions | umls-concept:C1155349 | lld:lifeskim |
| pubmed-article:18203838 | lifeskim:mentions | umls-concept:C1112870 | lld:lifeskim |
| pubmed-article:18203838 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:18203838 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:18203838 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:18203838 | pubmed:dateCreated | 2008-2-26 | lld:pubmed |
| pubmed-article:18203838 | pubmed:abstractText | Aer, the Escherichia coli aerotaxis receptor, faces the cytoplasm, where the PAS (Per-ARNT-Sim)-flavin adenine dinucleotide (FAD) domain senses redox changes in the electron transport system or cytoplasm. PAS-FAD interacts with a HAMP (histidine kinase, adenylyl cyclase, methyl-accepting protein, and phosphatase) domain to form an input-output module for Aer signaling. In this study, the structure of the Aer HAMP and proximal signaling domains was probed to elucidate structure-function relationships important for signaling. Aer residues 210 to 290 were individually replaced with cysteine and then cross-linked in vivo. The results confirmed that the Aer HAMP domain is composed of two alpha-helices separated by a structured loop. The proximal signaling domain consisted of two alpha-helices separated by a short undetermined structure. The Af1503 HAMP domain from Archaeoglobus fulgidus was recently shown to be a four-helix bundle. To test whether the Af1503 HAMP domain is a prototype for the Aer HAMP domain, the latter was modeled using coordinates from Af1503. Several findings supported the hypothesis that Aer has a four-helix HAMP structure: (i) cross-linking independently identified the same residues at the dimer interface that were predicted by the model, (ii) the rate of cross-linking for residue pairs was inversely proportional to the beta-carbon distances measured on the model, and (iii) clockwise lesions that were not contiguous in the linear Aer sequence were clustered in one region in the folded HAMP model, defining a potential site of PAS-HAMP interaction during signaling. In silico modeling of mutant Aer proteins indicated that the four-helix HAMP structure was important for Aer stability or maturation. The significance of the HAMP and proximal signaling domain structure for signal transduction is discussed. | lld:pubmed |
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| pubmed-article:18203838 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18203838 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18203838 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18203838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18203838 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18203838 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:18203838 | pubmed:issn | 1098-5530 | lld:pubmed |
| pubmed-article:18203838 | pubmed:author | pubmed-author:JohnsonMark... | lld:pubmed |
| pubmed-article:18203838 | pubmed:author | pubmed-author:WattsKylie... | lld:pubmed |
| pubmed-article:18203838 | pubmed:author | pubmed-author:TaylorBarry... | lld:pubmed |
| pubmed-article:18203838 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18203838 | pubmed:volume | 190 | lld:pubmed |
| pubmed-article:18203838 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18203838 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18203838 | pubmed:pagination | 2118-27 | lld:pubmed |
