|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==Crystal structure of C. albicans tRNA(His) guanylyltransferase (Thg1) with ATP== | | ==Crystal structure of C. albicans tRNA(His) guanylyltransferase (Thg1) with ATP== |
| - | <StructureSection load='3wbz' size='340' side='right' caption='[[3wbz]], [[Resolution|resolution]] 2.39Å' scene=''> | + | <StructureSection load='3wbz' size='340' side='right'caption='[[3wbz]], [[Resolution|resolution]] 2.39Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wbz]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Canal Canal]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WBZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WBZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wbz]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans_SC5314 Candida albicans SC5314]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WBZ 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></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]] 2.392Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wc0|3wc0]], [[3wc1|3wc1]], [[3wc2|3wc2]]</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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CaO19.7063, CAWG_05412, orf19.7063, THG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237561 CANAL])</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=3wbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wbz OCA], [https://pdbe.org/3wbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wbz RCSB], [https://www.ebi.ac.uk/pdbsum/3wbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wbz ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/tRNA(His)_guanylyltransferase tRNA(His) guanylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.79 2.7.7.79] </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=3wbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wbz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wbz RCSB], [http://www.ebi.ac.uk/pdbsum/3wbz PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| Line 17: |
Line 16: |
| | 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 3wbz" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Canal]] | + | [[Category: Candida albicans SC5314]] |
| - | [[Category: Nakamura, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Nemoto, T]] | + | [[Category: Nakamura A]] |
| - | [[Category: Sonoda, T]] | + | [[Category: Nemoto T]] |
| - | [[Category: Tanaka, I]] | + | [[Category: Sonoda T]] |
| - | [[Category: Yamashita, K]] | + | [[Category: Tanaka I]] |
| - | [[Category: Yao, M]] | + | [[Category: Yamashita K]] |
| - | [[Category: Transferase]]
| + | [[Category: Yao M]] |
| Structural highlights
Publication Abstract from PubMed
Nucleotide polymerization proceeds in the forward (5'-3') direction. This tenet of the central dogma of molecular biology is found in diverse processes including transcription, reverse transcription, DNA replication, and even in lagging strand synthesis where reverse polymerization (3'-5') would present a "simpler" solution. Interestingly, reverse (3'-5') nucleotide addition is catalyzed by the tRNA maturation enzyme tRNA(His) guanylyltransferase, a structural homolog of canonical forward polymerases. We present a Candida albicans tRNA(His) guanylyltransferase-tRNA(His) complex structure that reveals the structural basis of reverse polymerization. The directionality of nucleotide polymerization is determined by the orientation of approach of the nucleotide substrate. The tRNA substrate enters the enzyme's active site from the opposite direction (180 degrees flip) compared with similar nucleotide substrates of canonical 5'-3' polymerases, and the finger domains are on opposing sides of the core palm domain. Structural, biochemical, and phylogenetic data indicate that reverse polymerization appeared early in evolution and resembles a mirror image of the forward process.
Structural basis of reverse nucleotide polymerization.,Nakamura A, Nemoto T, Heinemann IU, Yamashita K, Sonoda T, Komoda K, Tanaka I, Soll D, Yao M Proc Natl Acad Sci U S A. 2013 Dec 24;110(52):20970-5. doi:, 10.1073/pnas.1321312111. Epub 2013 Dec 9. PMID:24324136[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nakamura A, Nemoto T, Heinemann IU, Yamashita K, Sonoda T, Komoda K, Tanaka I, Soll D, Yao M. Structural basis of reverse nucleotide polymerization. Proc Natl Acad Sci U S A. 2013 Dec 24;110(52):20970-5. doi:, 10.1073/pnas.1321312111. Epub 2013 Dec 9. PMID:24324136 doi:http://dx.doi.org/10.1073/pnas.1321312111
|
