5dku: Difference between revisions
New page: '''Unreleased structure''' The entry 5dku is ON HOLD Authors: Milton, ME, Honzatko, RB, Choe, JY, Nelson, SW Description: Category: Unreleased Structures [[Category: Milton, Me, H... |
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The | ==C-terminal His tagged apPOL exonuclease mutant== | ||
<StructureSection load='5dku' size='340' side='right'caption='[[5dku]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5dku]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DKU FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5dku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dku OCA], [https://pdbe.org/5dku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dku RCSB], [https://www.ebi.ac.uk/pdbsum/5dku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dku ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8ILY1_PLAF7 Q8ILY1_PLAF7] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Plasmodium falciparum, the primary cause of malaria, contains a non-photosynthetic plastid called the apicoplast. The apicoplast exists in most members of the phylum Apicomplexa and has its own genome along with organelle-specific enzymes for its replication. The only DNA polymerase found in the apicoplast (apPOL) was putatively acquired through horizontal gene transfer from a bacteriophage and is classified as an atypical A-family polymerase. Here, we present its crystal structure at a resolution of 2.9A. P. falciparum apPOL, the first structural representative of a plastidic A-family polymerase, diverges from typical A-family members in two of three previously identified signature motifs and in a region not implicated by sequence. Moreover, apPOL has an additional N-terminal subdomain, the absence of which severely diminishes its 3' to 5' exonuclease activity. A compound known to be toxic to Plasmodium is a potent inhibitor of apPOL, suggesting that apPOL is a viable drug target. The structure provides new insights into the structural diversity of A-family polymerases and may facilitate structurally guided antimalarial drug design. | |||
Crystal Structure of the Apicoplast DNA Polymerase from Plasmodium falciparum: The First Look at a Plastidic A-Family DNA Polymerase.,Milton ME, Choe JY, Honzatko RB, Nelson SW J Mol Biol. 2016 Jul 31. pii: S0022-2836(16)30274-1. doi:, 10.1016/j.jmb.2016.07.016. PMID:27487482<ref>PMID:27487482</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Milton | <div class="pdbe-citations 5dku" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Plasmodium falciparum 3D7]] | |||
[[Category: Choe JY]] | |||
[[Category: Honzatko RB]] | |||
[[Category: Milton ME]] | |||
[[Category: Nelson SW]] | |||
Latest revision as of 00:46, 29 June 2023
C-terminal His tagged apPOL exonuclease mutantC-terminal His tagged apPOL exonuclease mutant
Structural highlights
FunctionPublication Abstract from PubMedPlasmodium falciparum, the primary cause of malaria, contains a non-photosynthetic plastid called the apicoplast. The apicoplast exists in most members of the phylum Apicomplexa and has its own genome along with organelle-specific enzymes for its replication. The only DNA polymerase found in the apicoplast (apPOL) was putatively acquired through horizontal gene transfer from a bacteriophage and is classified as an atypical A-family polymerase. Here, we present its crystal structure at a resolution of 2.9A. P. falciparum apPOL, the first structural representative of a plastidic A-family polymerase, diverges from typical A-family members in two of three previously identified signature motifs and in a region not implicated by sequence. Moreover, apPOL has an additional N-terminal subdomain, the absence of which severely diminishes its 3' to 5' exonuclease activity. A compound known to be toxic to Plasmodium is a potent inhibitor of apPOL, suggesting that apPOL is a viable drug target. The structure provides new insights into the structural diversity of A-family polymerases and may facilitate structurally guided antimalarial drug design. Crystal Structure of the Apicoplast DNA Polymerase from Plasmodium falciparum: The First Look at a Plastidic A-Family DNA Polymerase.,Milton ME, Choe JY, Honzatko RB, Nelson SW J Mol Biol. 2016 Jul 31. pii: S0022-2836(16)30274-1. doi:, 10.1016/j.jmb.2016.07.016. PMID:27487482[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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