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The role of an extended beta‐sheet in stabilizing the structure of a thermophilic intein
Author(s) -
Colelli Kathryn M.,
Pusztay Jennifer M.,
Reitter Julie N.,
Mills Kenneth V.
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.1005.2
Subject(s) - intein , mutant , chemistry , protein splicing , thermophile , biochemistry , rna splicing , enzyme , gene , rna
Inteins are intervening polypeptides that are excised during the process of protein splicing, by which the intein is removed and the flanking polypeptides are ligated (N‐ and C‐ exteins). The Pyrococcus abyssi (Pab) PolII intein only splices at elevated temperatures. An NMR structure of the intein recently was solved in a collaborator's lab; the NMR data suggest increased rigidity of the intein in comparison to a mesophilic intein from Mycobacterium tuberculosis (Mtu), as well as a β‐hairpin found in inteins from archaebacteria. We have shown that mutations within the hairpin, which is distant from the active site, can both decrease the rate of catalysis as well as globally destabilize the structure of the protein. This material is based upon work supported by the National Science Foundation under grant MCB‐0950245, the Camille and Henry Dreyfus Foundation (KVM), and the Arnold and Mae Beckman Foundation (KMC).