3VXK

Crystal structure of OsD14

Summary for 3VXK

• Entry DOI: 10.2210/pdb3vxk/pdb
• Descriptor: Dwarf 88 esterase (2 entities in total)
• Functional Keywords: alpha/beta-hydrolase fold, hydrolase
• Biological source: Oryza sativa Japonica Group (Japanese rice)
• Cellular location: Cytoplasm : Q10QA5
• Total number of polymer chains: 2
• Total formula weight: 60048.72

Authors

Xue, Y.-L.,Miyakawa, T.,Hou, F.,Qin, H.-M.,Tanokura, M. (deposition date: 2012-09-18, release date: 2013-09-25, Last modification date: 2023-11-08)

Primary citation

Nakamura, H.,Xue, Y.-L.,Miyakawa, T.,Hou, F.,Qin, H.-M.,Fukui, K.,Shi, X.,Ito, E.,Ito, S.,Park, S.-H.,Miyauchi, Y.,Asano, A.,Totsuka, N.,Ueda, T.,Tanokura, M.,Asami, T.
Molecular mechanism of strigolactone perception by DWARF14
Nat Commun, 4:2613-2613, 2013

PubMed Abstract: Strigolactones (SLs) are phytohormones that inhibit shoot branching and function in the rhizospheric communication with symbiotic fungi and parasitic weeds. An α/β-hydrolase protein, DWARF14 (D14), has been recognized to be an essential component of plant SL signalling, although its precise function remains unknown. Here we present the SL-dependent interaction of D14 with a gibberellin signalling repressor SLR1 and a possible mechanism of phytohormone perception in D14-mediated SL signalling. D14 functions as a cleavage enzyme of SLs, and the cleavage reaction induces the interaction with SLR1. The crystal structure of D14 shows that 5-hydroxy-3-methylbutenolide (D-OH), which is a reaction product of SLs, is trapped in the catalytic cavity of D14 to form an altered surface. The D14 residues recognizing D-OH are critical for the SL-dependent D14-SLR1 interaction. These results provide new insight into crosstalk between gibberellin and SL signalling pathways.

PubMed: 24131983
DOI: 10.1038/ncomms3613

Experimental method

X-RAY DIFFRACTION (1.75 Å)