2jmz
Solution structure of a KlbA intein precursor from Methanococcus jannaschii
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OverviewOverview
Certain proteins of unicellular organisms are translated as precursor, polypeptides containing inteins (intervening proteins), which are domains, capable of performing protein splicing. These domains, in conjunction with, a single residue following the intein, catalyze their own excision from, the surrounding protein (extein) in a multistep reaction involving the, cleavage of two intein-extein peptide bonds and the formation of a new, peptide bond that ligates the two exteins to yield the mature protein. We, report here the solution NMR structure of a 186-residue precursor of the, KlbA intein from Methanococcus jannaschii, comprising the intein together, with N- and C-extein segments of 7 and 11 residues, respectively. The, intein is shown to adopt a single, well-defined globular domain, representing a HINT (Hedgehog/Intein)-type topology. Fourteen beta-strands, are arranged in a complex fold that includes four beta-hairpins and an, antiparallel beta-ribbon, and there is one alpha-helix, which is packed, against the beta-ribbon, and one turn of 3(10)-helix in the loop between, the beta-strands 8 and 9. The two extein segments show increased disorder, and form only minimal nonbonding contacts with the intein domain., Structure-based mutation experiments resulted in a proposal for functional, roles of individual residues in the intein catalytic mechanism.
About this StructureAbout this Structure
2JMZ is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
ReferenceReference
NMR structure of a KlbA intein precursor from Methanococcus jannaschii., Johnson MA, Southworth MW, Herrmann T, Brace L, Perler FB, Wuthrich K, Protein Sci. 2007 Jul;16(7):1316-28. PMID:17586768
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