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| | <StructureSection load='6q52' size='340' side='right'caption='[[6q52]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='6q52' size='340' side='right'caption='[[6q52]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6q52]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_24743 Dsm 24743]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q52 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6q52]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Planococcus_halocryophilus Planococcus halocryophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q52 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2TM:5-O-[(S)-HYDROXY{[(S)-HYDROXY(PHOSPHONOOXY)PHOSPHORYL]METHYL}PHOSPHORYL]CYTIDINE'>2TM</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]] 2.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BBI08_05760 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1215089 DSM 24743])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2TM:5-O-[(S)-HYDROXY{[(S)-HYDROXY(PHOSPHONOOXY)PHOSPHORYL]METHYL}PHOSPHORYL]CYTIDINE'>2TM</scene></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=6q52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q52 OCA], [https://pdbe.org/6q52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q52 RCSB], [https://www.ebi.ac.uk/pdbsum/6q52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q52 ProSAT]</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=6q52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q52 OCA], [http://pdbe.org/6q52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q52 RCSB], [http://www.ebi.ac.uk/pdbsum/6q52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q52 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A1C7DQ98_9BACL A0A1C7DQ98_9BACL]] 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.[SAAS:SAAS00711016] | + | [https://www.uniprot.org/uniprot/A0A1C7DQ98_9BACL A0A1C7DQ98_9BACL] 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.[SAAS:SAAS00711016] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6q52" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6q52" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[CCA-adding enzyme 3D structures|CCA-adding enzyme 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: CCA tRNA nucleotidyltransferase]] | |
| - | [[Category: Dsm 24743]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Betat, H]] | + | [[Category: Planococcus halocryophilus]] |
| - | [[Category: Bluhm, A]] | + | [[Category: Betat H]] |
| - | [[Category: Hennig, O]] | + | [[Category: Bluhm A]] |
| - | [[Category: Lorber, B]] | + | [[Category: Hennig O]] |
| - | [[Category: Moerl, M]] | + | [[Category: Lorber B]] |
| - | [[Category: Rollet, K]] | + | [[Category: Moerl M]] |
| - | [[Category: Sauter, C]] | + | [[Category: Rollet K]] |
| - | [[Category: Wijn, R de]] | + | [[Category: Sauter C]] |
| - | [[Category: Chipx]]
| + | [[Category: De Wijn R]] |
| - | [[Category: Psychrophilic enzyme]]
| + | |
| - | [[Category: Rna binding protein]]
| + | |
| - | [[Category: Trna maturation]]
| + | |
| - | [[Category: Trna nucleotidyltransferase]]
| + | |
| Structural highlights
Function
A0A1C7DQ98_9BACL 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.[SAAS:SAAS00711016]
Publication Abstract from PubMed
Determining optimal conditions for the production of well diffracting crystals is a key step in every biocrystallography project. Here, a microfluidic device is described that enables the production of crystals by counter-diffusion and their direct on-chip analysis by serial crystallography at room temperature. Nine 'non-model' and diverse biomacromolecules, including seven soluble proteins, a membrane protein and an RNA duplex, were crystallized and treated on-chip with a variety of standard techniques including micro-seeding, crystal soaking with ligands and crystal detection by fluorescence. Furthermore, the crystal structures of four proteins and an RNA were determined based on serial data collected on four synchrotron beamlines, demonstrating the general applicability of this multipurpose chip concept.
A simple and versatile microfluidic device for efficient biomacromolecule crystallization and structural analysis by serial crystallography.,de Wijn R, Hennig O, Roche J, Engilberge S, Rollet K, Fernandez-Millan P, Brillet K, Betat H, Morl M, Roussel A, Girard E, Mueller-Dieckmann C, Fox GC, Olieric V, Gavira JA, Lorber B, Sauter C IUCrJ. 2019 Apr 19;6(Pt 3):454-464. doi: 10.1107/S2052252519003622. eCollection, 2019 May 1. PMID:31098026[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ de Wijn R, Hennig O, Roche J, Engilberge S, Rollet K, Fernandez-Millan P, Brillet K, Betat H, Morl M, Roussel A, Girard E, Mueller-Dieckmann C, Fox GC, Olieric V, Gavira JA, Lorber B, Sauter C. A simple and versatile microfluidic device for efficient biomacromolecule crystallization and structural analysis by serial crystallography. IUCrJ. 2019 Apr 19;6(Pt 3):454-464. doi: 10.1107/S2052252519003622. eCollection, 2019 May 1. PMID:31098026 doi:http://dx.doi.org/10.1107/S2052252519003622
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