2a6a
Crystal structure of Glycoprotein endopeptidase (tm0874) from THERMOTOGA MARITIMA at 2.50 A resolution
Structural highlights
FunctionTSAB_THEMA Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) 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 t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedYeaZ 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. 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. 2010 Oct 1;66(Pt, 10):1230-6. Epub 2009 Oct 27. PMID:20944216[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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