2zh6: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Complex structure of AFCCA with tRNAminiDCU and ATP== | ==Complex structure of AFCCA with tRNAminiDCU and ATP== | ||
<StructureSection load='2zh6' size='340' side='right' caption='[[2zh6]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2zh6' size='340' side='right'caption='[[2zh6]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zh6]] 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=2ZH6 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[2zh6]] 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=2ZH6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZH6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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]], [[2zh5|2zh5]], [[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]], [[2zh5|2zh5]], [[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:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2zh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zh6 OCA], [http://pdbe.org/2zh6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zh6 RCSB], [http://www.ebi.ac.uk/pdbsum/2zh6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zh6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 31: | Line 31: | ||
==See Also== | ==See Also== | ||
*[[CCA-adding enzyme|CCA-adding enzyme]] | *[[CCA-adding enzyme 3D structures|CCA-adding enzyme 3D structures]] | ||
*[[ | *[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 38: | Line 38: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arcfl]] | [[Category: Arcfl]] | ||
[[Category: Large Structures]] | |||
[[Category: Toh, Y]] | [[Category: Toh, Y]] | ||
[[Category: Tomita, K]] | [[Category: Tomita, K]] | ||
Revision as of 15:04, 29 July 2020
Complex structure of AFCCA with tRNAminiDCU and ATPComplex structure of AFCCA with tRNAminiDCU and ATP
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
|
| ||||||||||||||||||