Title: | Crystal structure of Glycoprotein endopeptidase (tm0874) from THERMOTOGA MARITIMA at 2.50 A resolution |
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Classification: | HYDROLASE |
Technique: | X-Ray Diffraction |
Resolution: | 2.50 |
R value free: | 0.235 |
R value observed: | |
R value work: | 0.191 |
Pdb Files | 2A6A.pdb 6N9A.pdb 6S84.pdb |
Pdbx/mmCIF Files | 2A6A.cif 6N9A.cif 6S84.cif |
MNVLALDTSQRIRIGLRKGEDLFEISYTGEKKHAEILPVVVKKLLDELDLKVKDLDVVGVGIGPGGLTGLRVGIATVVGLVSPYDIPVAPLNSFEMTAKSCPADGVVLVARRARKGYHYCAVYLKDKGLNPLKEPSVVSDEELEEITKEFSPKIVLKDDLLISPAVLVEESERLFREKKTIHYYEIEPLYLQKSIAELNWEKKKRG
In bacteria four proteins: TsaD, Sua5, TsaE and TsaB (YgjD, YrdC, YjeE, and YeaZ, respectively) are both necessary and sufficient for t6A biosynthesis in vitro. YrdC and YgjD are members of universally conserved families while YeaZ and YjeE are specific to bacteria. TsaB shows homology with YgjD (TsaD) and interacts physically with YjeE (TsaE) and YgjD (TsaD). together with YjeE, TsaB may also regulate the activity of YgjD. Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE; this reaction does not require ATP in vitro. TsaB seems to play an indirect role in the t6A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD (By similarity) [ANNOTATED FROM UNIPROT]
Enter the variants
Position
Original
Variant
Alpha Fold Pdb Files | AF-Q9WZX7-F1.pdb |
Alpha Fold Pdbx/mmCIF Files | AF-Q9WZX7-F1.cif |
DSSP Secondary Structures | Q9WZX7.dssp |