TY - JOUR
T1 - Structural dissection of the maltodextrin disproportionation cycle of the Arabidopsis plastidial disproportionating enzyme 1 (DPE1)
AU - O'Neill, Ellis C.
AU - Stevenson, Clare E.M.
AU - Tantanarat, Krit
AU - Latousakis, Dimitrios
AU - Donaldson, Matthew I.
AU - Rejzek, Martin
AU - Nepogodiev, Sergey A.
AU - Limpaseni, Tipaporn
AU - Field, Robert A.
AU - Lawson, David M.
N1 - Publisher Copyright:
© 2015 by The American Society for Biochemistry and Molecular Biology, Inc. Published in the U.S.A.
PY - 2015/12/11
Y1 - 2015/12/11
N2 - Background: Arabidopsis maltodextrin disproportionating enzyme 1 (AtDPE1) plays a key role in chloroplast starch degradation. Results: Six AtDPE1 structures define the active site and reveal mechanistically relevant conformations of both the enzyme and substrate. Conclusion: Substrates are captured through loop rearrangements; the subtle deployment of active site residues controls catalysis. Significance: A molecular level understanding of the complete disproportionation cycle of AtDPE1 is presented.
AB - Background: Arabidopsis maltodextrin disproportionating enzyme 1 (AtDPE1) plays a key role in chloroplast starch degradation. Results: Six AtDPE1 structures define the active site and reveal mechanistically relevant conformations of both the enzyme and substrate. Conclusion: Substrates are captured through loop rearrangements; the subtle deployment of active site residues controls catalysis. Significance: A molecular level understanding of the complete disproportionation cycle of AtDPE1 is presented.
UR - http://www.scopus.com/inward/record.url?scp=84949636198&partnerID=8YFLogxK
U2 - 10.1074/jbc.M115.682245
DO - 10.1074/jbc.M115.682245
M3 - Article
C2 - 26504082
AN - SCOPUS:84949636198
VL - 290
SP - 29834
EP - 29853
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 50
ER -