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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1j5u ConSurf]. | ||
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Revision as of 03:20, 8 February 2016
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
Function[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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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