An alpha/beta barrel is a protein fold formed by units composed of a short α-helix followed by two anti-parallel β-strands, followed by an α-helix and a β-strand; the three β-strands form a β-sheet that runs parallel to the barrel and the α-helix is in the outside of the barrel but does not contact the α-helices of the other repeats like in TIM barrels.
The protein structures known for this fold come proteins from the eukaryotic and archaeal initiation factor 6 family, namely the Methanococcus jannaschii aIF6 and Saccharomyces cerevisiae eIF6,[1] and from the eIF6 from Dictyostelium discoideum.[2]
These alpha/beta barrels are commonly occurring motifs constructed from repetitions of the beta-alpha-beta loop motif. This alpha/beta barrel is a domain of pyruvate kinase enzyme. [3]
References
- ^ Groft CM, Beckmann R, Sali A, Burley SK (December 2000). "Crystal structures of ribosome anti-association factor IF6". Nat. Struct. Biol. 7 (12): 1156–64. doi:10.1038/82017. PMID 11101899. S2CID 35762049.
- ^ Weis F, Giudice E, Churcher M, Jin L, Hilcenko C, Wong CC, Traynor D, Kay RR, Warren AJ (November 2015). "Mechanism of eIF6 release from the nascent 60S ribosomal subunit". Nat. Struct. Mol. Biol. 22 (11): 914–9. doi:10.1038/nsmb.3112. PMC 4871238. PMID 26479198.
- ^ Lee, J. C.; Herman, P. (2011). Structural and functional energetic linkages in allosteric regulation of muscle pyruvate kinase. Methods in Enzymology. Vol. 488. pp. 185–217. doi:10.1016/B978-0-12-381268-1.00008-2. ISBN 9780123812681. PMID 21195229.
This page was last edited on 1 September 2023, at 21:14