2JMZ
Solution structure of a KlbA intein precursor from Methanococcus jannaschii
Summary for 2JMZ
| Entry DOI | 10.2210/pdb2jmz/pdb |
| Descriptor | Hypothetical protein MJ0781 (1 entity in total) |
| Functional Keywords | protein, unknown function |
| Biological source | Methanocaldococcus jannaschii |
| Cellular location | Membrane; Single-pass membrane protein (Potential): Q58191 |
| Total number of polymer chains | 1 |
| Total formula weight | 21441.24 |
| Authors | Johnson, M.A.,Southworth, M.W.,Herrmann, T.,Brace, L.,Perler, F.B.,Wuthrich, K.A. (deposition date: 2006-12-14, release date: 2007-07-10, Last modification date: 2023-12-20) |
| Primary citation | Johnson, M.A.,Southworth, M.W.,Herrmann, T.,Brace, L.,Perler, F.B.,Wuthrich, K. NMR structure of a KlbA intein precursor from Methanococcus jannaschii Protein Sci., 16:1316-1328, 2007 Cited by PubMed Abstract: 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. PubMed: 17586768DOI: 10.1110/ps.072816707 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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