2jnq: Difference between revisions
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<StructureSection load='2jnq' size='340' side='right' caption='[[2jnq]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | <StructureSection load='2jnq' size='340' side='right' caption='[[2jnq]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jnq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2jnq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JNQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JNQ FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jmz|2jmz]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jmz|2jmz]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jnq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jnq RCSB], [http://www.ebi.ac.uk/pdbsum/2jnq PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jnq OCA], [http://pdbe.org/2jnq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jnq RCSB], [http://www.ebi.ac.uk/pdbsum/2jnq PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2jnq" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Atcc 43067]] | ||
[[Category: Brace, L]] | [[Category: Brace, L]] | ||
[[Category: Herrmann, T]] | [[Category: Herrmann, T]] | ||
Revision as of 03:20, 10 September 2015
Solution Structure of a KlbA Intein Precursor from Methanococcus jannaschiiSolution Structure of a KlbA Intein Precursor from Methanococcus jannaschii
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCertain 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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