Structural mechanism of abscisic acid binding and signaling by dimeric PYR1.
Structural mechanism of abscisic acid binding and signaling by dimeric PYR1.
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DOI:
10.1126/science.1181829
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发表时间:
2009-12-04
期刊:
影响因子:
--
通讯作者:
Getzoff ED
中科院分区:
文献类型:
--
作者:
Nishimura N;Hitomi K;Arvai AS;Rambo RP;Hitomi C;Cutler SR;Schroeder JI;Getzoff ED
The phytohormone abscisic acid (ABA) acts in seed dormancy, plant development, drought tolerance and adaptive responses to environmental stresses. Structural mechanisms mediating ABA receptor recognition and signaling remain unknown, but are essential for understanding and manipulating abiotic stress resistance. Here we report structures of PYR1, a prototypical PYR/PYL/RCAR protein that functions in early ABA signaling. The crystallographic structure reveals an α/β helix-grip fold and homodimeric assembly, verified in vivo by co-immunoprecipitation. ABA binding within a large internal cavity switches structural motifs distinguishing ABA-free “open-lid” from ABA-bound “closed-lid” conformations. Small angle X-ray scattering suggests that ABA signals by converting PYR1 to a more compact, symmetric closed-lid dimer. Site-directed PYR1 mutants designed to disrupt hormone binding lose ABA-triggered interactions with type 2C protein phosphatase partners in planta.
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DOI:
10.1126/science.1173041
发表时间:
2009-05-22
期刊:
Science (New York, N.Y.)
影响因子:
--
作者:
Park SY;Fung P;Nishimura N;Jensen DR;Fujii H;Zhao Y;Lumba S;Santiago J;Rodrigues A;Chow TF;Alfred SE;Bonetta D;Finkelstein R;Provart NJ;Desveaux D;Rodriguez PL;McCourt P;Zhu JK;Schroeder JI;Volkman BF;Cutler SR
通讯作者:
Cutler SR
影响因子:
56.9
作者:
MEYER, K;LEUBE, MP;GRILL, E
通讯作者:
GRILL, E
影响因子:
11.6
作者:
Leonhardt, N;Kwak, JM;Schroeder, JI
通讯作者:
Schroeder, JI
影响因子:
64.8
作者:
EAGLES, CF;WAREING, PF
通讯作者:
WAREING, PF
影响因子:
56.9
作者:
LEUNG, J;BOUVIERDURAND, M;GIRAUDAT, J
通讯作者:
GIRAUDAT, J