| pubmed-article:9761469 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9761469 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:9761469 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:9761469 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:9761469 | lifeskim:mentions | umls-concept:C1441672 | lld:lifeskim |
| pubmed-article:9761469 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:9761469 | lifeskim:mentions | umls-concept:C0439836 | lld:lifeskim |
| pubmed-article:9761469 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:9761469 | pubmed:dateCreated | 1998-12-14 | lld:pubmed |
| pubmed-article:9761469 | pubmed:abstractText | The conversion from an alpha-helix to a beta-strand has received extensive attention since this structural change may induce many amyloidogenic proteins to self-assemble into fibrils and cause fatal diseases. Here we report the conversion of a peptide segment from a beta-strand to an alpha-helix by a single-site mutation as observed in the crystal structure of Fis mutant Pro26Ala determined at 2.0 A resolution. Pro26 in Fis occurs at the point where a flexible extended beta-hairpin arm leaves the core structure. Thus it can be classified as a "hinge proline" located at the C-terminal end of the beta2-strand and the N-terminal cap of the A alpha-helix. The replacement of Pro26 to alanine extends the A alpha-helix for two additional turns in one of the dimeric subunits; therefore, the structure of the peptide from residues 22 to 26 is converted from a beta-strand to an alpha-helix. This result confirms the structural importance of the proline residue located at the hinge region and may explain the mutant's reduced ability to activate Hin-catalyzed DNA inversion. The peptide (residues 20 to 26) in the second monomer subunit presumably retains its beta-strand conformation in the crystal; therefore, this peptide shows a "chameleon-like" character since it can adopt either an alpha-helix or a beta-strand structure in different environments. The structure of Pro26Ala provides an additional example where not only the protein sequence, but also non-local interactions determine the secondary structure of proteins. | lld:pubmed |
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| pubmed-article:9761469 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9761469 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9761469 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9761469 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9761469 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:9761469 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:9761469 | pubmed:author | pubmed-author:JohnsonR CRC | lld:pubmed |
| pubmed-article:9761469 | pubmed:author | pubmed-author:LIT ITI | lld:pubmed |
| pubmed-article:9761469 | pubmed:author | pubmed-author:YangW ZWZ | lld:pubmed |
| pubmed-article:9761469 | pubmed:author | pubmed-author:YuanH SHS | lld:pubmed |
| pubmed-article:9761469 | pubmed:author | pubmed-author:CorselliLL | lld:pubmed |
| pubmed-article:9761469 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9761469 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:9761469 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9761469 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9761469 | pubmed:pagination | 1875-83 | lld:pubmed |
| pubmed-article:9761469 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9761469 | pubmed:meshHeading | pubmed-meshheading:9761469-... | lld:pubmed |
| pubmed-article:9761469 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9761469 | pubmed:articleTitle | Conversion of a beta-strand to an alpha-helix induced by a single-site mutation observed in the crystal structure of Fis mutant Pro26Ala. | lld:pubmed |
| pubmed-article:9761469 | pubmed:affiliation | Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan, Republic of China. | lld:pubmed |
| pubmed-article:9761469 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9761469 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9761469 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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