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| | ==Solution Structures of RadA intein from Pyrococcus horikoshii== | | ==Solution Structures of RadA intein from Pyrococcus horikoshii== |
| - | <StructureSection load='2lqm' size='340' side='right'caption='[[2lqm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lqm' size='340' side='right'caption='[[2lqm]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lqm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lqm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQM FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4e2u|4e2u]], [[4e2t|4e2t]]</div></td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lqm OCA], [https://pdbe.org/2lqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lqm RCSB], [https://www.ebi.ac.uk/pdbsum/2lqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lqm ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DNA repair and recombination protein RadA, PH0263, radA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70601 Pyrococcus horikoshii])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lqm OCA], [https://pdbe.org/2lqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lqm RCSB], [https://www.ebi.ac.uk/pdbsum/2lqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lqm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RADA_PYRHO RADA_PYRHO]] Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (By similarity).
| + | [https://www.uniprot.org/uniprot/RADA_PYRHO RADA_PYRHO] Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pyrococcus horikoshii]] | + | [[Category: Pyrococcus horikoshii OT3]] |
| - | [[Category: Iwai, H]] | + | [[Category: Iwai H]] |
| - | [[Category: Kajander, T]] | + | [[Category: Kajander T]] |
| - | [[Category: Oeemig, J S]] | + | [[Category: Oeemig JS]] |
| - | [[Category: Wlodawer, A]] | + | [[Category: Wlodawer A]] |
| - | [[Category: Zhou, D]] | + | [[Category: Zhou D]] |
| - | [[Category: Unknown function]]
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| Structural highlights
Function
RADA_PYRHO Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (By similarity).
Publication Abstract from PubMed
In protein splicing, an intervening protein sequence (intein) in the host protein excises itself out and ligates two split host protein sequences (exteins) to produce a mature host protein. Inteins require the involvement for the splicing of the first residue of the extein that follows the intein (which is Cys, Ser, or Thr). Other extein residues near the splicing junctions could modulate splicing efficiency even when they are not directly involved in catalysis. Mutual interdependence between this molecular parasite (intein) and its host protein (exteins) is not beneficial for intein spread but could be advantageous for intein survival during evolution. Elucidating extein-intein dependency has increasingly become important since inteins are recognized as useful biotechnological tools for protein ligation. We determined the structures of one of inteins with high splicing efficiency, the RadA intein from Pyrococcus horikoshii (PhoRadA). The solution NMR structure and the crystal structures elucidated the structural basis for its high efficiency and directed our efforts of engineering that led to rational design of a functional minimized RadA intein. The crystal structure of the minimized RadA intein also revealed the precise interactions between N-extein and the intein. We systematically analyzed the effects at the -1 position of N-extein and were able to significantly improve the splicing efficiency of a less robust splicing variant by eliminating the unfavorable extein-intein interactions observed in the structure. This work provides an example of how unveiling structure-function relationships of inteins offer a promising way of improving their properties as better tools for protein engineering.
NMR and Crystal Structures of the Pyrococcus horikoshii RadA Intein Guide a Strategy for Engineering a Highly Efficient and Promiscuous Intein.,Oeemig JS, Zhou D, Kajander T, Wlodawer A, Iwai H J Mol Biol. 2012 Aug 3;421(1):85-99. Epub 2012 May 2. PMID:22560994[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Oeemig JS, Zhou D, Kajander T, Wlodawer A, Iwai H. NMR and Crystal Structures of the Pyrococcus horikoshii RadA Intein Guide a Strategy for Engineering a Highly Efficient and Promiscuous Intein. J Mol Biol. 2012 Aug 3;421(1):85-99. Epub 2012 May 2. PMID:22560994 doi:10.1016/j.jmb.2012.04.029
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