7oec: Difference between revisions
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==Crystal structure of an intein from a hyperthermophile== | ==Crystal structure of an intein from a hyperthermophile== | ||
<StructureSection load='7oec' size='340' side='right'caption='[[7oec]]' scene=''> | <StructureSection load='7oec' size='340' side='right'caption='[[7oec]], [[Resolution|resolution]] 1.48Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OEC FirstGlance]. <br> | <table><tr><td colspan='2'>[[7oec]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OEC FirstGlance]. <br> | ||
</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=7oec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oec OCA], [https://pdbe.org/7oec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oec RCSB], [https://www.ebi.ac.uk/pdbsum/7oec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oec ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=7oec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oec OCA], [https://pdbe.org/7oec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oec RCSB], [https://www.ebi.ac.uk/pdbsum/7oec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oec ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/DP2L_PYRHO DP2L_PYRHO] Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Inteins are prevalent among extremophiles. Mini-inteins with robust splicing properties are of particular interest for biotechnological applications due to their small size. However, biochemical and structural characterization has still been limited to a small number of inteins, and only a few serve as widely used tools in protein engineering. We determined the crystal structure of a naturally occurring Pol-II mini-intein from Pyrococcus horikoshii and compared all three mini-inteins found in the genome of P. horikoshii. Despite their similar sizes, the comparison revealed distinct differences in the insertions and deletions, implying specific evolutionary pathways from distinct ancestral origins. Our studies suggest that sporadically distributed mini-inteins might be more promising for further protein engineering applications than highly conserved mini-inteins. Structural investigations of additional inteins could guide the shortest path to finding novel robust mini-inteins suitable for various protein engineering purposes. | |||
Mini-Intein Structures from Extremophiles Suggest a Strategy for Finding Novel Robust Inteins.,Hiltunen MK, Beyer HM, Iwai H Microorganisms. 2021 Jun 5;9(6). pii: microorganisms9061226. doi:, 10.3390/microorganisms9061226. PMID:34198729<ref>PMID:34198729</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7oec" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Pyrococcus horikoshii OT3]] | |||
[[Category: Hannes B]] | [[Category: Hannes B]] | ||
[[Category: Hiltunen M]] | [[Category: Hiltunen M]] | ||
[[Category: Iwai H]] | [[Category: Iwai H]] | ||
Latest revision as of 14:03, 15 November 2023
Crystal structure of an intein from a hyperthermophileCrystal structure of an intein from a hyperthermophile
Structural highlights
FunctionDP2L_PYRHO Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity). Publication Abstract from PubMedInteins are prevalent among extremophiles. Mini-inteins with robust splicing properties are of particular interest for biotechnological applications due to their small size. However, biochemical and structural characterization has still been limited to a small number of inteins, and only a few serve as widely used tools in protein engineering. We determined the crystal structure of a naturally occurring Pol-II mini-intein from Pyrococcus horikoshii and compared all three mini-inteins found in the genome of P. horikoshii. Despite their similar sizes, the comparison revealed distinct differences in the insertions and deletions, implying specific evolutionary pathways from distinct ancestral origins. Our studies suggest that sporadically distributed mini-inteins might be more promising for further protein engineering applications than highly conserved mini-inteins. Structural investigations of additional inteins could guide the shortest path to finding novel robust mini-inteins suitable for various protein engineering purposes. Mini-Intein Structures from Extremophiles Suggest a Strategy for Finding Novel Robust Inteins.,Hiltunen MK, Beyer HM, Iwai H Microorganisms. 2021 Jun 5;9(6). pii: microorganisms9061226. doi:, 10.3390/microorganisms9061226. PMID:34198729[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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