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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2005-3-28
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pubmed:abstractText |
The structural properties of the linker peptide connecting the cellulose-binding module to the catalytic module in bimodular cellulases have been investigated by small-angle x-ray scattering. Since the linker and the cellulose-binding module are relatively small and cannot be readily detected separately, the conformation of the linker was studied by means of an artificial fusion protein, Cel6BA, in which an 88-residue linker connects the large catalytic modules of the cellulases Cel6A and Cel6B from Humicola insolens. Our data showed that Cel6BA is very elongated with a maximum dimension of 178 A, but could not be described by a single conformation. Modeling of a series of Cel6BA conformers with interdomain separations ranging between 10 A and 130 A showed that good Guinier and P(r) profile fits were obtained by a weighted average of the scattering curves of all the models where the linker follows a nonrandom distribution, with a preference for the more compact conformers. These structural properties are likely to be essential for the function of the linker as a molecular spring between the two functional modules. Small-angle x-ray scattering therefore provides a unique tool to quantitatively analyze the conformational disorder typical of proteins described as natively unfolded.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-10064707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-10550212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-10794732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-10884353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-10962023,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-11784292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-11804721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-12186865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-12368089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-12418105,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-12496082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-12621042,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-14670951,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-1886523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-1904063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-2744487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-3045756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-3894007,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-6310128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-7578050,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15653742-9882628
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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 |
Apr
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pubmed:issn |
0006-3495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2823-32
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pubmed:dateRevised |
2010-9-21
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pubmed:meshHeading |
pubmed-meshheading:15653742-Amino Acid Sequence,
pubmed-meshheading:15653742-Ascomycota,
pubmed-meshheading:15653742-Biophysics,
pubmed-meshheading:15653742-Catalytic Domain,
pubmed-meshheading:15653742-Cellulase,
pubmed-meshheading:15653742-Cellulose,
pubmed-meshheading:15653742-Hydrolysis,
pubmed-meshheading:15653742-Models, Molecular,
pubmed-meshheading:15653742-Models, Statistical,
pubmed-meshheading:15653742-Molecular Conformation,
pubmed-meshheading:15653742-Molecular Sequence Data,
pubmed-meshheading:15653742-Protein Conformation,
pubmed-meshheading:15653742-Protein Structure, Tertiary,
pubmed-meshheading:15653742-Proteins,
pubmed-meshheading:15653742-Recombinant Fusion Proteins,
pubmed-meshheading:15653742-Scattering, Radiation,
pubmed-meshheading:15653742-X-Rays
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pubmed:year |
2005
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pubmed:articleTitle |
Protein disorder: conformational distribution of the flexible linker in a chimeric double cellulase.
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pubmed:affiliation |
Novozymes A/S, Bagsvaerd, Denmark.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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