Modomics - A Database of RNA Modifications

ID Card:

Full name: tRNA threonylcarbamoyladenosine biosynthesis protein TsaB
Synonym: YeaZ
GI: 15643636
COG: COG1214
UniProt: Q9WZX7
Structures: | 2A6A | 6N9A | 6S84 |
Alpha Fold Predicted Structure: AF-Q9WZX7-F1
Enzyme type: endopeptidase predicted
Position of modification - modification: t:37 - t6A


PDB Structures:


2A6A

Structure Description:

Title:
Classification:
Technique:

Abstract of the PDB Structure's related Publication:

YeaZ is involved in a protein network that is essential for bacteria. The crystal structure of YeaZ from Thermotoga maritima was determined to 2.5 A resolution. Although this protein belongs to a family of ancient actin-like ATPases, it appears that it has lost the ability to bind ATP since it lacks some key structural features that are important for interaction with ATP. A conserved surface was identified, supporting its role in the formation of protein complexes.

Download RCSB-PDB Structures:

Pdb Files   2A6A.pdb   6N9A.pdb   6S84.pdb  
Pdbx/mmCIF Files   2A6A.cif   6N9A.cif   6S84.cif  


Protein sequence:

MNVLALDTSQRIRIGLRKGEDLFEISYTGEKKHAEILPVVVKKLLDELDLKVKDLDVVGVGIGPGGLTGLRVGIATVVGLVSPYDIPVAPLNSFEMTAKSCPADGVVLVARRARKGYHYCAVYLKDKGLNPLKEPSVVSDEELEEITKEFSPKIVLKDDLLISPAVLVEESERLFREKKTIHYYEIEPLYLQKSIAELNWEKKKRG

Comments:

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]





Alpha Fold Predicted Structure:






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Protein sequence:


Secondary Structure Alphabet

  • G: 3-turn helix (310helix)
  • H: α-helix
  • I: 𝝅-helix (5 - turn helix)
  • T: Hydrogen Bonded Turn
  • B: β-sheet
  • S: Bend
  • C: Coil (residues not present in any of the above conformations)
  • N: Not assigned

Download PDB Structures & DSSP Secondary Structures:

Alpha Fold Pdb Files   AF-Q9WZX7-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-Q9WZX7-F1.cif  
DSSP Secondary Structures   Q9WZX7.dssp  





Publications:

Title Authors Journal Details PubMed Id DOI
Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 A resolution. Xu Q, McMullan D, Jaroszewski L, Krishna SS, Elsliger MA, Yeh AP, Abdubek P, Astakhova T, Axelrod HL, Carlton D, Chiu HJ, Clayton T, Duan L, Feuerhelm J, Grant J, Han GW, Jin KK, Klock HE, Knuth MW, Miller MD, Morse AT, Nigoghossian E, Okach L, Oommachen S, Paulsen J, Reyes R, Rife CL, van den Bedem H, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA Acta Crystallogr Sect F Struct Biol Cryst Commun [details] 20944216 -