4wc2: Difference between revisions
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<StructureSection load='4wc2' size='340' side='right' caption='[[4wc2]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='4wc2' size='340' side='right' caption='[[4wc2]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wc2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WC2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WC2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4wc2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WC2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WC2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vfg|1vfg]], [[4wby|4wby]], [[4wbz|4wbz]], [[4wc0|4wc0]], [[4wc1|4wc1]], [[4wc3|4wc3]], [[4wc4|4wc4]], [[4wc5|4wc5]], [[4wc6|4wc6]], [[4wc7|4wc7]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vfg|1vfg]], [[4wby|4wby]], [[4wbz|4wbz]], [[4wc0|4wc0]], [[4wc1|4wc1]], [[4wc3|4wc3]], [[4wc4|4wc4]], [[4wc5|4wc5]], [[4wc6|4wc6]], [[4wc7|4wc7]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pcnB1, aq_411 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wc2 OCA], [http://pdbe.org/4wc2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wc2 RCSB], [http://www.ebi.ac.uk/pdbsum/4wc2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wc2 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wc2 OCA], [http://pdbe.org/4wc2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wc2 RCSB], [http://www.ebi.ac.uk/pdbsum/4wc2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wc2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4wc2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4wc2" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aquae]] | |||
[[Category: Tomita, K]] | [[Category: Tomita, K]] | ||
[[Category: Yamashita, S]] | [[Category: Yamashita, S]] | ||
Revision as of 15:11, 6 November 2017
Crystal structure of tRNA nucleotidyltransferase complexed with a primer tRNA and an incoming ATP analogCrystal structure of tRNA nucleotidyltransferase complexed with a primer tRNA and an incoming ATP analog
Structural highlights
Publication Abstract from PubMedThe 3'-terminal CCA (C74C75A76-3') of tRNA is required for protein synthesis. In Aquifex aeolicus, the CCA-3' is synthesized by CC-adding and A-adding enzymes, although in most organisms, CCA is synthesized by a single CCA-adding enzyme. The mechanisms by which the A-adding enzyme adds only A76, but not C74C75, onto tRNA remained elusive. The complex structures of the enzyme with various tRNAs revealed the presence of a single tRNA binding site on the enzyme, with the enzyme measuring the acceptor-TPsiC helix length of tRNA. The 3'-C75 of tRNA lacking A76 can reach the active site and the size and shape of the nucleotide binding pocket at the insertion stage are suitable for ATP. The 3'-C74 of tRNA lacking C75A76 cannot reach the active site, although CTP or ATP can bind the active pocket. Thus, the A-adding enzyme adds only A76, but not C74C75, onto tRNA. Measurement of Acceptor-TPsiC Helix Length of tRNA for Terminal A76-Addition by A-Adding Enzyme.,Yamashita S, Martinez A, Tomita K Structure. 2015 May 5;23(5):830-42. doi: 10.1016/j.str.2015.03.013. Epub 2015 Apr, 23. PMID:25914059[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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