5hyz
Crystal Structure of SCL7 in Oryza sativa
Structural highlights
FunctionSCL7_ORYSJ Probable transcription factor involved in plant development (By similarity). Involved in environmental abiotic stress resistance. May increase the expression of stress-responsive genes (By similarity). Binds DNA in vitro (PubMed:27081181).[UniProtKB:A0A024B7I0][UniProtKB:Q9SCR0][1] Publication Abstract from PubMedGRAS proteins belong to a plant-specific protein family with many members and play essential roles in plant growth and development, functioning primarily in transcriptional regulation. Proteins in the family are minimally defined as containing the conserved GRAS domain. Here we have determined the structure of the GRAS domain of Os-SCL7 from Oryza sativa to 1.82A. The structure includes cap and core sub-domains, and elucidates the features of the conserved GRAS LRI, VHIID, LRII, PFYRE, and SAW motifs. The structure is a dimer, with a clear groove to accommodate double-stranded DNA. Docking a DNA segment into the groove to generate an Os-SCL7/DNA complex provides insight into the DNA binding mechanism of GRAS proteins. Furthermore, the in vitro DNA binding property of Os-SCL7 and model-defined recognition residues are assessed by EMSA analysis and mutagenesis assays. These studies reveal the structure and preliminary DNA interaction mechanisms of GRAS proteins and open the door to in-depth investigation and understanding of the individual pathways in which they play important roles. Crystal structure of the GRAS domain of SCARECROW-LIKE 7 in Oryza sativa.,Li S, Zhao Y, Zhao Z, Wu X, Sun L, Liu Q, Wu Y Plant Cell. 2016 Apr 14. pii: tpc.00018.2016. PMID:27081181[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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