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| | <StructureSection load='3h38' size='340' side='right'caption='[[3h38]], [[Resolution|resolution]] 2.37Å' scene=''> | | <StructureSection load='3h38' size='340' side='right'caption='[[3h38]], [[Resolution|resolution]] 2.37Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3h38]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H38 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3H38 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3h38]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H38 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3h37|3h37]], [[3h39|3h39]], [[3h3a|3h3a]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.37Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/CCA_tRNA_nucleotidyltransferase CCA tRNA nucleotidyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.72 2.7.7.72] </span></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=3h38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h38 OCA], [https://pdbe.org/3h38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h38 RCSB], [https://www.ebi.ac.uk/pdbsum/3h38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h38 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3h38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h38 OCA], [http://pdbe.org/3h38 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h38 RCSB], [http://www.ebi.ac.uk/pdbsum/3h38 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3h38 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9WZH4_THEMA Q9WZH4_THEMA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43589]] | |
| - | [[Category: CCA tRNA nucleotidyltransferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Toh, Y]] | + | [[Category: Thermotoga maritima]] |
| - | [[Category: Tomita, K]] | + | [[Category: Toh Y]] |
| - | [[Category: Nucleotide-binding]] | + | [[Category: Tomita K]] |
| - | [[Category: Nucleotidyltransferase]]
| + | |
| - | [[Category: Rna-binding]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transferase/rna]]
| + | |
| Structural highlights
Function
Q9WZH4_THEMA
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 PubMed
The CCA-adding enzyme synthesizes the CCA sequence at the 3' end of tRNA without a nucleic acid template. The crystal structures of class II Thermotoga maritima CCA-adding enzyme and its complexes with CTP or ATP were determined. The structure-based replacement of both the catalytic heads and nucleobase-interacting neck domains of the phylogenetically closely related Aquifex aeolicus A-adding enzyme by the corresponding domains of the T. maritima CCA-adding enzyme allowed the A-adding enzyme to add CCA in vivo and in vitro. However, the replacement of only the catalytic head domain did not allow the A-adding enzyme to add CCA, and the enzyme exhibited (A, C)-adding activity. We identified the region in the neck domain that prevents (A, C)-adding activity and defines the number of nucleotide incorporations and the specificity for correct CCA addition. We also identified the region in the head domain that defines the terminal A addition after CC addition. The results collectively suggest that, in the class II CCA-adding enzyme, the head and neck domains collaboratively and dynamically define the number of nucleotide additions and the specificity of nucleotide selection.
Mechanism for the definition of elongation and termination by the class II CCA-adding enzyme.,Toh Y, Takeshita D, Numata T, Fukai S, Nureki O, Tomita K EMBO J. 2009 Nov 4;28(21):3353-65. Epub 2009 Sep 10. PMID:19745807[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Toh Y, Takeshita D, Numata T, Fukai S, Nureki O, Tomita K. Mechanism for the definition of elongation and termination by the class II CCA-adding enzyme. EMBO J. 2009 Nov 4;28(21):3353-65. Epub 2009 Sep 10. PMID:19745807 doi:10.1038/emboj.2009.260
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