Linked Life Data

20225260

Source:http://linkedlifedata.com/resource/pubmed/id/20225260

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2010-4-21
pubmed:databankReference
pubmed:abstractText
B. cereus HlyIIR belongs to the TetR family of dimeric transcriptional regulators. Unlike other members of the TetR family, HlyIIR contains an insert between alpha-helices alpha8 and alpha9, which is located at the subunit-subunit interface. N-terminal segment of this insert (amino acids, Pro161-Ser169) forms a short alpha-helix alpha8* that occupies a complementary cavity on the surface of the adjacent subunit, whereas the C-terminal segment comprising 16 amino acids (Leu170-Glu185) is disordered. To understand whether this disordered segment is important for protein's function, we determined crystal structures of two engineered HlyIIR proteins where this segment was either substituted by a seven-residue flexible Ser-Gly linker or replaced by a cleavable peptide containing proteolytic sites at both ends. Unexpectedly, alteration or proteolytic removal of the disordered segment resulted in changes in protein's conformation and in a remarkable rearrangement at the subunit-subunit interface. X-ray structures of the two engineered proteins revealed an unusual plasticity at the dimerization interface of HlyIIR enabling it to form dimers stabilized by different sets of interactions. Structural comparison indicates that in spite of the flexible nature of the disordered segment, it is critical for maintaining the native structure as it influences the position of alpha8*. The data demonstrate how disordered loops on protein surfaces may affect folding and subunit-subunit interactions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1097-0134
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1870-7
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Structural investigation of transcriptional regulator HlyIIR: influence of a disordered region on protein fold and dimerization.
pubmed:affiliation
York Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, United Kingdom. oleg@ysbl.york.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't