A novel main chain motif in proteins bridged by cationic groups: the niche.
We have surveyed the bridging of pairs of main chain carbonyl oxygens by cations or by delta(+) hydrogens within hydrogen bonding groups. A three to four residue motif, which we call the niche, with characteristic phi,psi angles, is by far the commonest feature with this property. The niche accommodates atoms or groups that offer delta(+) charges, including water molecules or metal ions, as well as amines, guanidines, and other NH(2) groups. Seven percent of all residues in an average soluble protein belong to a niche; another 7% have the niche conformation but no obvious bridging delta(+) group. Fifty-five percent of niches occur either following a type 1 beta-turn or at the C-termini of alpha-helices, and niches turn out to be the most common C-terminal features of alpha-helices: 39% of alpha-helical C-termini are niches, whereas 34% are Schellman loops. 3(10) helices also frequently terminate in niches. Niches that bind K(+), Na(+) or Ca(2+) occur in some functional contexts: in the cyclic peptides valinomycin and antamanide; in several enzymes that are allosterically activated by Na(+) or K(+); and in the calcium pump, where a niche is integrally involved in the ion transport.
Torrance
Gilleain M
GM
Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow, G12 8QQ, UK.
Leader
David P
DP
Gilbert
David R
DR
Milner-White
E James
EJ
D000465:Algorithms; D020816:Amino Acid Motifs; D000596:Amino Acids / Q000378:metabolism; D002412:Cations; D016000:Cluster Analysis; D004926:Escherichia coli / Q000201:enzymology; D008670:Metals / Q000378:metabolism; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
D000596:Amino Acids; D002412:Cations; D008670:Metals; D011506:Proteins