7oec: Difference between revisions

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<StructureSection load='7oec' size='340' side='right'caption='[[7oec]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
<StructureSection load='7oec' size='340' side='right'caption='[[7oec]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7oec]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. 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='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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 1.48&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">polC, PH0121 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70601 Pyrococcus horikoshii])</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>
<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 ==
== 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).  
[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;">
<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: Hannes, B]]
[[Category: Hannes B]]
[[Category: Hiltunen, M]]
[[Category: Hiltunen M]]
[[Category: Iwai, H]]
[[Category: Iwai H]]
[[Category: Intein]]
[[Category: Protein splicing]]
[[Category: Splicing]]

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

7oec is a 1 chain structure with sequence from Pyrococcus horikoshii OT3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.48Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

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[1]

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

References

  1. Hiltunen MK, Beyer HM, Iwai H. Mini-Intein Structures from Extremophiles Suggest a Strategy for Finding Novel Robust Inteins. Microorganisms. 2021 Jun 5;9(6). pii: microorganisms9061226. doi:, 10.3390/microorganisms9061226. PMID:34198729 doi:http://dx.doi.org/10.3390/microorganisms9061226

7oec, resolution 1.48Å

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