4kl5: Difference between revisions
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==Crystal structure of NpuDnaE intein== | |||
=== | <StructureSection load='4kl5' size='340' side='right' caption='[[4kl5]], [[Resolution|resolution]] 1.72Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4kl5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nosp7 Nosp7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KL5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KL5 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2keq|2keq]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DnaE N- and C-intein part, Npun_F4872 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63737 NOSP7])</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4kl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kl5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kl5 RCSB], [http://www.ebi.ac.uk/pdbsum/4kl5 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein sequences are diversified on the DNA level by recombination and mutation and can be further increased on the RNA level by alternative RNA splicing, involving introns that have important roles in many biological processes. The protein version of introns (inteins), which catalyze protein splicing, were first reported in the 1990s. The biological roles of protein splicing still remain elusive because inteins neither provide any clear benefits nor have an essential role in their host organisms. We now report protein alternative splicing, in which new protein sequences can be produced by protein recombination by intermolecular domain swapping of inteins, as elucidated by NMR spectroscopy and crystal structures. We demonstrate that intein-mediated protein alternative splicing could be a new strategy to increase protein diversity (that is, functions) without any modification in genetic backgrounds. We also exploited it as a post-translational protein conformation-driven switch of protein functions (for example, as highly specific protein interference). | |||
Intermolecular domain swapping induces intein-mediated protein alternative splicing.,Aranko AS, Oeemig JS, Kajander T, Iwai H Nat Chem Biol. 2013 Aug 25. doi: 10.1038/nchembio.1320. PMID:23974115<ref>PMID:23974115</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
==See Also== | |||
*[[DNA polymerase|DNA polymerase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: DNA-directed DNA polymerase]] | [[Category: DNA-directed DNA polymerase]] | ||
[[Category: | [[Category: Nosp7]] | ||
[[Category: Aranko, A S.]] | [[Category: Aranko, A S.]] | ||
[[Category: Iwai, H.]] | [[Category: Iwai, H.]] | ||
Revision as of 09:22, 11 June 2014
Crystal structure of NpuDnaE inteinCrystal structure of NpuDnaE intein
Structural highlights
Publication Abstract from PubMedProtein sequences are diversified on the DNA level by recombination and mutation and can be further increased on the RNA level by alternative RNA splicing, involving introns that have important roles in many biological processes. The protein version of introns (inteins), which catalyze protein splicing, were first reported in the 1990s. The biological roles of protein splicing still remain elusive because inteins neither provide any clear benefits nor have an essential role in their host organisms. We now report protein alternative splicing, in which new protein sequences can be produced by protein recombination by intermolecular domain swapping of inteins, as elucidated by NMR spectroscopy and crystal structures. We demonstrate that intein-mediated protein alternative splicing could be a new strategy to increase protein diversity (that is, functions) without any modification in genetic backgrounds. We also exploited it as a post-translational protein conformation-driven switch of protein functions (for example, as highly specific protein interference). Intermolecular domain swapping induces intein-mediated protein alternative splicing.,Aranko AS, Oeemig JS, Kajander T, Iwai H Nat Chem Biol. 2013 Aug 25. doi: 10.1038/nchembio.1320. PMID:23974115[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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