2zh3: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
==Complex structure of AFCCA with tRNAminiDCA== | ==Complex structure of AFCCA with tRNAminiDCA== | ||
<StructureSection load='2zh3' size='340' side='right' caption='[[2zh3]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2zh3' size='340' side='right' caption='[[2zh3]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zh3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2zh3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZH3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZH3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zh1|2zh1]], [[2zh2|2zh2]], [[2zh4|2zh4]], [[2zh5|2zh5]], [[2zh6|2zh6]], [[2zh7|2zh7]], [[2zh8|2zh8]], [[2zh9|2zh9]], [[2zha|2zha]], [[2zhb|2zhb]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zh1|2zh1]], [[2zh2|2zh2]], [[2zh4|2zh4]], [[2zh5|2zh5]], [[2zh6|2zh6]], [[2zh7|2zh7]], [[2zh8|2zh8]], [[2zh9|2zh9]], [[2zha|2zha]], [[2zhb|2zhb]]</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=2zh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zh3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zh3 RCSB], [http://www.ebi.ac.uk/pdbsum/2zh3 PDBsum]</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=2zh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zh3 OCA], [http://pdbe.org/2zh3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zh3 RCSB], [http://www.ebi.ac.uk/pdbsum/2zh3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zh3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
Line 17: | Line 18: | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2zh3 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Line 27: | Line 28: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2zh3" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[CCA-adding enzyme|CCA-adding enzyme]] | *[[CCA-adding enzyme|CCA-adding enzyme]] | ||
*[[TRNA|TRNA]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Arcfl]] | ||
[[Category: Toh, Y]] | [[Category: Toh, Y]] | ||
[[Category: Tomita, K]] | [[Category: Tomita, K]] |
Revision as of 01:06, 6 August 2016
Complex structure of AFCCA with tRNAminiDCAComplex structure of AFCCA with tRNAminiDCA
Structural highlights
Function[CCA_ARCFU] Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCCA-adding enzyme builds the 3'-end CCA of tRNA without a nucleic acid template. The mechanism for the maintenance of fidelity during the CCA-adding reaction remains elusive. Here, we present almost a dozen complex structures of the class I CCA-adding enzyme and tRNA mini-helices (mini-D(73)N(74), mini-D(73)N(74)C(75) and mini-D(73)C(74)N(75); D(73) is a discriminator nucleotide and N is either A, G, or U). The mini-D(73)N(74) complexes adopt catalytically inactive open forms, and CTP shifts the enzymes to the active closed forms and allows N(74) to flip for CMP incorporation. In contrast, unlike the catalytically active closed form of the mini-D(73)C(74)C(75) complex, the mini-D(73)N(74)C(75) and mini-D(73)C(74)N(75) complexes adopt inactive open forms. Only the mini-D(73)C(74)U(75) accepts AMP to a similar extent as mini-D(73)C(74)C(75), and ATP shifts the enzyme to a closed, active form and allows U(75) to flip for AMP incorporation. These findings suggest that the 3'-region of RNA is proofread, after two nucleotide additions, in the closed, active form of the complex at the AMP incorporation stage. This proofreading is a prerequisite for the maintenance of fidelity for complete CCA synthesis. Molecular basis for maintenance of fidelity during the CCA-adding reaction by a CCA-adding enzyme.,Toh Y, Numata T, Watanabe K, Takeshita D, Nureki O, Tomita K EMBO J. 2008 Jul 23;27(14):1944-52. Epub 2008 Jun 26. PMID:18583961[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|