Protein Science, Vol 3, Issue 11 1927-1937, Copyright © 1994 by Cold Spring Harbor Laboratory Press

ARTICLE

The tyrosine corner: A feature of most Greek key {beta}-barrel proteins

J. M. HEMMINGSEN, K. M. GERNERT, J. S. RICHARDSON and D. C. RICHARDSON
Department of Biochemistry, Duke University, Durham, North Carolina 27710

The Tyr corner is a conformation in which a tyrosine (residue ``Y'') near the beginning or end of an antiparallel {beta}-strand makes an H bond from its side-chain OH group to the backbone NH and/or CO of residue Y -- 3, Y -- 4, or Y -- 5 in the nearby connection. The most common ``classic'' case is a {Delta}4 Tyr corner (more than 40 examples listed), in which the H bond is to residue Y -- 4 and the Tyr ({chi})1 is near --60{deg}. Y -- 2 is almost always a glycine, whose left-handed {beta} or very extended {beta} conformation helps the backbone curve around the Tyr ring. Residue Y -- 3 is in polyproline II conformation (often Pro), and residue Y -- 5 is usually a hydrophobic (often Leu) that packs next to the Tyr ring. The consensus sequence, then, is LxPGxY, where the first x (the H-bonding position) is hydrophilic. Residues Y and Y -- 2 both form narrow pairs of {beta}-sheet H-bonds with the neighboring strand. {Delta}5 Tyr corners have a 1-residue insertion between the Gly and the Tyr, forming a {beta}-bulge. One protein family has a {Delta}4 corner formed by a His rather than a Tyr, and several examples use Trp in place of Tyr. For almost all these cases, the protein or domain is a Greek key {beta}-barrel structure, the Tyr corner ends a Greek key connection, and it is well-conserved in related proteins. Most low-twist Greek key {beta}-barrels have 1 Tyr corner. ``Reverse'' {Delta}4 Tyr corners (H bonded to Y + 4) and other variants are described, all less common and less conserved. It seems likely that the more classic Tyr corners ({Delta}4, {Delta}5, and {Delta}3 Tyr, Trp, or His) contribute to the stability of a Greek key connection over a hairpin connection, and also that they may aid in the process of folding up Greek key structures.
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