2jmz: Difference between revisions

Revision as of 19:04, 21 February 2008

Solution structure of a KlbA intein precursor from Methanococcus jannaschii

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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OCA

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 ==Overview==
-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.
+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 Structure==
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 [[Category: Brace, L.]]
 [[Category: Herrmann, T.]]
-[[Category: Johnson, M.A.]]
+[[Category: Johnson, M A.]]
-[[Category: Perler, F.B.]]
+[[Category: Perler, F B.]]
-[[Category: Southworth, M.W.]]
+[[Category: Southworth, M W.]]
-[[Category: Wuthrich, K.A.]]
+[[Category: Wuthrich, K A.]]
 [[Category: protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:35:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:04:16 2008''