4ohv: Difference between revisions
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==C. Elegans Clp1 bound to AMP-PNP, and Mg2+== | ==C. Elegans Clp1 bound to AMP-PNP, and Mg2+== | ||
<StructureSection load='4ohv' size='340' side='right' caption='[[4ohv]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='4ohv' size='340' side='right'caption='[[4ohv]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ohv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OHV OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4ohv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OHV FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4ohv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ohv OCA], [https://pdbe.org/4ohv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ohv RCSB], [https://www.ebi.ac.uk/pdbsum/4ohv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ohv ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CLP1_CAEEL CLP1_CAEEL] Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Caenorhabditis elegans]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Clausen T]] | ||
[[Category: | [[Category: Dikfidan A]] | ||
[[Category: | [[Category: Loll B]] | ||
[[Category: | [[Category: Meinhart A]] | ||
[[Category: | [[Category: Zeymer C]] | ||
Latest revision as of 14:14, 6 November 2024
C. Elegans Clp1 bound to AMP-PNP, and Mg2+C. Elegans Clp1 bound to AMP-PNP, and Mg2+
Structural highlights
FunctionCLP1_CAEEL Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation (By similarity). Publication Abstract from PubMedRNA-specific polynucleotide kinases of the Clp1 subfamily are key components of various RNA maturation pathways. However, the structural basis explaining their substrate specificity and the enzymatic mechanism is elusive. Here, we report crystal structures of Clp1 from Caenorhabditis elegans (ceClp1) in a number of nucleotide- and RNA-bound states along the reaction pathway. The combined structural and biochemical analysis of ceClp1 elucidates the RNA specificity and lets us derive a general model for enzyme catalysis of RNA-specific polynucleotide kinases. We identified an RNA binding motif referred to as "clasp" as well as a conformational switch that involves the essential Walker A lysine (Lys127) and regulates the enzymatic activity of ceClp1. Structural comparison with other P loop proteins, such as kinases, adenosine triphosphatases (ATPases), and guanosine triphosphatases (GTPases), suggests that the observed conformational switch of the Walker A lysine is a broadly relevant mechanistic feature. RNA specificity and regulation of catalysis in the eukaryotic polynucleotide kinase clp1.,Dikfidan A, Loll B, Zeymer C, Magler I, Clausen T, Meinhart A Mol Cell. 2014 Jun 19;54(6):975-86. doi: 10.1016/j.molcel.2014.04.005. Epub 2014 , May 8. PMID:24813946[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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