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Science 9 October 1987:
Vol. 238. no. 4824, pp. 205 - 208
DOI: 10.1126/science.238.4824.205
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Articles

An Amylose Antiparallel Double Helix at Atomic Resolution

W. HINRICHS 1, G. BÜTTNER 1, M. STEIFA 1, CH. BETZEL 1, V. ZABEL 1, B. PFANNEMÜLLER 2, and W. SAENGER 1

1 Institut für Kristallographic, Freie Universität Berlin, Takustrasse 6, D-1000 Berlin 33, Federal Republic of Germany.
2 Institut für Makromolekulare Chemie, Universität Freiburg, Stefan-Meier-Strasse 31, 7800 D-7800 Freiburg, Federal Republic of Germany.

In the crystal structure of the polyiodide complex (p-nitrophenyl-agr-maltohexaose2) · Ba(I3)2 · 22H2O, the maltohexaose units form an antiparallel, left-handed double helix with O-2 ... O-3 and O-6 ... O-6 hydrogen bonding and a central cavity that encloses two triiodide units. This structure contrasts with the parallel, left-handed double helix with no central cavity proposed for the A-and B-starch helix and the left-handed single helix in V-amylose and may be relevant for the stabilization of glycogen Structure.

Submitted on February 27, 1987
Accepted on July 7, 1987


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The Cyclization Mechanism of Cyclodextrin Glycosyltransferase (CGTase) as Revealed by a gamma -Cyclodextrin-CGTase Complex at 1.8-A Resolution.
J. C. M. Uitdehaag, K. H. Kalk, B. A. van der Veen, L. Dijkhuizen, and B. W. Dijkstra (1999)
J. Biol. Chem. 274, 34868-34876
   Abstract »    Full Text »    PDF »
V-Amylose at atomic resolution: X-ray structure of a cycloamylose with 26 glucose residues (cyclomaltohexaicosaose).
K. Gessler, I. Uson, T. Takaha, N. Krauss, S. M. Smith, S. Okada, G. M. Sheldrick, and W. Saenger (1999)
PNAS 96, 4246-4251
   Abstract »    Full Text »    PDF »
Potato D-enzyme Catalyzes the Cyclization of Amylose to Produce Cycloamylose, a Novel Cyclic Glucan.
T. Takaha, M. Yanase, H. Takata, S. Okada, and S. M. Smith (1996)
J. Biol. Chem. 271, 2902-2908
   Abstract »    Full Text »    PDF »


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