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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
1998-12-14
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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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-1484481,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-1619650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-1668651,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-1834996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-1851089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-1946369,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-1986310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-2166334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-2237415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-3381086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-3524854,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-3536909,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-7603994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-7670375,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-7768815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-7913765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-7961857,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-8078589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-8117669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-8503008,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-8614471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-8696966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-8700211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-8939740,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-8980678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-9007987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-9032055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-9083108,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-9204889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9761469-9362499
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1875-83
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9761469-Amino Acid Sequence,
pubmed-meshheading:9761469-Bacterial Proteins,
pubmed-meshheading:9761469-Carrier Proteins,
pubmed-meshheading:9761469-Crystallography, X-Ray,
pubmed-meshheading:9761469-Dimerization,
pubmed-meshheading:9761469-Disulfides,
pubmed-meshheading:9761469-Escherichia coli,
pubmed-meshheading:9761469-Escherichia coli Proteins,
pubmed-meshheading:9761469-Factor For Inversion Stimulation Protein,
pubmed-meshheading:9761469-Integration Host Factors,
pubmed-meshheading:9761469-Models, Molecular,
pubmed-meshheading:9761469-Molecular Sequence Data,
pubmed-meshheading:9761469-Mutation,
pubmed-meshheading:9761469-Protein Structure, Secondary
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pubmed:year |
1998
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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.
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pubmed:affiliation |
Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan, Republic of China.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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