1j5u: Difference between revisions
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<StructureSection load='1j5u' size='340' side='right'caption='[[1j5u]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1j5u' size='340' side='right'caption='[[1j5u]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1j5u]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1j5u]] 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=1J5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J5U FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1j5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j5u OCA], [https://pdbe.org/1j5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j5u RCSB], [https://www.ebi.ac.uk/pdbsum/1j5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j5u ProSAT], [https://www.topsan.org/Proteins/JCSG/1j5u TOPSAN]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ARCH_THEMA ARCH_THEMA] Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity). May also act as a chaperone or modulator of proteins involved in DNA or RNA processing. | ||
== 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: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermotoga maritima]] | ||
Latest revision as of 02:43, 28 December 2023
CRYSTAL STRUCTURE OF AN ARCHEASE, POSSIBLE CHAPERONE (TM1083) FROM THERMOTOGA MARITIMA AT 2.0 A RESOLUTIONCRYSTAL STRUCTURE OF AN ARCHEASE, POSSIBLE CHAPERONE (TM1083) FROM THERMOTOGA MARITIMA AT 2.0 A RESOLUTION
Structural highlights
FunctionARCH_THEMA Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity). May also act as a chaperone or modulator of proteins involved in DNA or RNA processing. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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