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==Crystal structure of NpuDnaE intein==
==Crystal structure of NpuDnaE intein==
<StructureSection load='4kl5' size='340' side='right' caption='[[4kl5]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
<StructureSection load='4kl5' size='340' side='right' caption='[[4kl5]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
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<tr id='gene'><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 id='gene'><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 id='activity'><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 id='activity'><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 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=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>
<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=4kl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kl5 OCA], [http://pdbe.org/4kl5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kl5 RCSB], [http://www.ebi.ac.uk/pdbsum/4kl5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kl5 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4kl5" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Revision as of 16:58, 4 August 2016

Crystal structure of NpuDnaE inteinCrystal structure of NpuDnaE intein

Structural highlights

4kl5 is a 2 chain structure with sequence from Nosp7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:DnaE N- and C-intein part, Npun_F4872 (NOSP7)
Activity:DNA-directed DNA polymerase, with EC number 2.7.7.7
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Aranko AS, Oeemig JS, Kajander T, Iwai H. Intermolecular domain swapping induces intein-mediated protein alternative splicing. Nat Chem Biol. 2013 Aug 25. doi: 10.1038/nchembio.1320. PMID:23974115 doi:10.1038/nchembio.1320

4kl5, resolution 1.72Å

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