Biology:Alpha beta barrel
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
- ↑ "Crystal structures of ribosome anti-association factor IF6". Nat. Struct. Biol. 7 (12): 1156–64. December 2000. doi:10.1038/82017. PMID 11101899.
- ↑ "Mechanism of eIF6 release from the nascent 60S ribosomal subunit". Nat. Struct. Mol. Biol. 22 (11): 914–9. November 2015. doi:10.1038/nsmb.3112. PMID 26479198.
- ↑ Lee, J. C.; Herman, P. (2011). Structural and functional energetic linkages in allosteric regulation of muscle pyruvate kinase. Methods in Enzymology. 488. pp. 185–217. doi:10.1016/B978-0-12-381268-1.00008-2. ISBN 9780123812681.
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