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.
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. PMID11101899. S2CID35762049.
^Lee, J. C.; Herman, P. (2011). "Structural and Functional Energetic Linkages in Allosteric Regulation of Muscle Pyruvate Kinase". Biothermodynamics, Part C. Methods in Enzymology. Vol. 488. pp. 185–217. doi:10.1016/B978-0-12-381268-1.00008-2. ISBN9780123812681. PMID21195229.
