2zh5: Difference between revisions
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==Complex structure of AFCCA with tRNAminiDCU== | ==Complex structure of AFCCA with tRNAminiDCU== | ||
<StructureSection load='2zh5' size='340' side='right' caption='[[2zh5]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='2zh5' size='340' side='right' caption='[[2zh5]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
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</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]], [[2zh3|2zh3]], [[2zh4|2zh4]], [[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]], [[2zh3|2zh3]], [[2zh4|2zh4]], [[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=2zh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zh5 OCA], [http://pdbe.org/2zh5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zh5 RCSB], [http://www.ebi.ac.uk/pdbsum/2zh5 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=2zh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zh5 OCA], [http://pdbe.org/2zh5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zh5 RCSB], [http://www.ebi.ac.uk/pdbsum/2zh5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zh5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zh/2zh5_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zh/2zh5_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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==See Also== | ==See Also== | ||
*[[CCA-adding enzyme|CCA-adding enzyme]] | *[[CCA-adding enzyme|CCA-adding enzyme]] | ||
*[[TRNA|TRNA]] | |||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 09:50, 18 October 2018
Complex structure of AFCCA with tRNAminiDCUComplex structure of AFCCA with tRNAminiDCU
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
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