1987
DOI: 10.1073/pnas.84.15.5087
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Conformation of a 16-residue zervamicin IIA analog peptide containing three different structural features: 3(10)-helix, alpha-helix, and beta-bend ribbon.

Abstract: Boc-Trp-Ile-Ala-Aib-Ile-Val-Aib-Leu-AibPro-Ala-Aib-Pro-Aib-Pro-Phe-OMe (where Boc is t-butoxycarbonyl and Aib is a-aminoisobutyric acid), a synthetic apolar analog of the membrane-active fungal peptide antibiotic zervamycin IIA, crystallizes in space group P1 with Z = 1 and cell parameters a = 9.086 ± 0. angles Hi range from -51°to -91°(average value -64°), and the torsion angles Pif range from -1°to -46°(average value -31°). There are 10 intramolecular NH-..OC hydrogen bonds in the helix and two direct head-t… Show more

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Cited by 127 publications
(72 citation statements)
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“…Indeed, the -(Aib-L-Pro) n -sequence was shown to fold into a variant of the right-handed 3 10 -helix, known as the b-bend ribbon. 15,16 This helix is stabilized by 50% of the intramolecular H-bonds occurring in a regular 3 10 -helix. An additional property of Pro is that it occurs extensively in the collagen triple helix.…”
Section: Introductionmentioning
confidence: 99%
“…Indeed, the -(Aib-L-Pro) n -sequence was shown to fold into a variant of the right-handed 3 10 -helix, known as the b-bend ribbon. 15,16 This helix is stabilized by 50% of the intramolecular H-bonds occurring in a regular 3 10 -helix. An additional property of Pro is that it occurs extensively in the collagen triple helix.…”
Section: Introductionmentioning
confidence: 99%
“…Linear peptides form fl-sheets (Karle, Karle, Mastropaolo, Camerman & Camerman, 1983), 3,0-helices for short peptides (Toniolo et al, 1983), ahelices for longer peptides Fox & Richards, 1982), double helices (Benedetti, di Blasio, Pedone, Lorenzi, Tomasic & Gramlich, 1979;Langs, 1988) and mixed helices consisting of a 3,0/ahelix and a fl-ribbon twisted into a helix (Karle, Flippen-Anderson, Sukumar & Balaram, 1987;Karle, Flippen-Anderson, Agarwalla & Balaram, 1991). The latter has been established in Leu-zervamicin and a 16-residue apolar analog that contain in their sequences three Pro or Hyp (hydroxyproline) residues at positions 10, 13 and 15.…”
Section: Backbonesmentioning
confidence: 99%
“…The unusual conformation and the probable mobility of the Gln"1 side chain strongly suggest the location of the gating mechanism during ion transport (see below). Additionally, the polar face is enhanced by the exposed backbone carbonyl oxygens in residues 6, 7, and 10, which do not participate in intrahelical hydrogen bonds ( N (5) N (6) OY (6) N (7) N (8) N (9) 06 (10) (10) 0 (8) 0 (9) 0E (13) (12) is almost identical to that of the backbone in the natural [Leul]zervamicin. The configuration of the Iva residue at position 4 is R, confirming an earlier stereochemical assignment (8).…”
mentioning
confidence: 99%
“…The search model was based on the backbone atoms ofthe known structure ofa 16-residue apolar analog of zervamicin (12) and was followed by a partialstructure procedure (13) by which the atoms in the side chains were located. The detailed structure only of crystal A will be reported here.…”
mentioning
confidence: 99%