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1UL5

Solution structure of the DNA-binding domain of squamosa promoter binding protein-like 7

Summary for 1UL5
Entry DOI10.2210/pdb1ul5/pdb
Descriptorsquamosa promoter binding protein-like 7, ZINC ION (2 entities in total)
Functional Keywordstranscription factor, sbp, flower development, dna binding protein, structural genomics, riken structural genomics/proteomics initiative, rsgi
Biological sourceArabidopsis thaliana (thale cress)
Cellular locationNucleus (Probable): Q8S9G8
Total number of polymer chains1
Total formula weight10284.56
Authors
Yamasaki, K.,Inoue, M.,Kigawa, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-09-09, release date: 2004-03-09, Last modification date: 2023-12-27)
Primary citationYamasaki, K.,Kigawa, T.,Inoue, M.,Tateno, M.,Yamasaki, T.,Yabuki, T.,Aoki, M.,Seki, E.,Matsuda, T.,Nunokawa, E.,Ishizuka, Y.,Terada, T.,Shirouzu, M.,Osanai, T.,Tanaka, A.,Seki, M.,Shinozaki, K.,Yokoyama, S.
A novel zinc-binding motif revealed by solution structures of DNA-binding domains of Arabidopsis SBP-family transcription factors.
J.Mol.Biol., 337:49-63, 2004
Cited by
PubMed Abstract: SQUAMOSA promoter binding proteins (SBPs) form a major family of plant-specific transcription factors related to flower development. Although SBPs are heterogeneous in primary structure, they share a highly conserved DNA-binding domain (DBD) that has been suggested to be zinc binding. Here we report the NMR solution structures of DBDs of two SBPs of Arabidopsis thaliana, SPL4 and SPL7. The two share essentially the same structural features. Each structure contains two zinc-binding sites consisting of eight Cys or His residues in a Cys3HisCys2HisCys or Cys6HisCys sequence motif in which the first four residues coordinate to one zinc and the last four coordinate to the other. These structures are dissimilar to other known zinc-binding structures, and thus represent a novel type of zinc-binding motif. The electrostatic profile on the surface suggested that a continuous region, including all the conserved basic residues, is involved in the DNA binding, the mode of which is likely to be novel as well.
PubMed: 15001351
DOI: 10.1016/j.jmb.2004.01.015
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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數據於2024-11-13公開中

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