3UGM
Structure of TAL effector PthXo1 bound to its DNA target
Summary for 3UGM
| Entry DOI | 10.2210/pdb3ugm/pdb |
| Descriptor | TAL effector AvrBs3/PthA, DNA-1, DNA-2, ... (4 entities in total) |
| Functional Keywords | tal effector, transcription-dna complex, dna binding protein, transcription/dna |
| Biological source | Xanthomonas oryzae More |
| Total number of polymer chains | 3 |
| Total formula weight | 132292.32 |
| Authors | Mak, A.N.S.,Bradley, P.,Cernadas, R.A.,Bogdanove, A.J.,Stoddard, B.L. (deposition date: 2011-11-02, release date: 2012-01-04, Last modification date: 2024-02-28) |
| Primary citation | Mak, A.N.,Bradley, P.,Cernadas, R.A.,Bogdanove, A.J.,Stoddard, B.L. The Crystal Structure of TAL Effector PthXo1 Bound to Its DNA Target. Science, 335:716-719, 2012 Cited by PubMed Abstract: DNA recognition by TAL effectors is mediated by tandem repeats, each 33 to 35 residues in length, that specify nucleotides via unique repeat-variable diresidues (RVDs). The crystal structure of PthXo1 bound to its DNA target was determined by high-throughput computational structure prediction and validated by heavy-atom derivatization. Each repeat forms a left-handed, two-helix bundle that presents an RVD-containing loop to the DNA. The repeats self-associate to form a right-handed superhelix wrapped around the DNA major groove. The first RVD residue forms a stabilizing contact with the protein backbone, while the second makes a base-specific contact to the DNA sense strand. Two degenerate amino-terminal repeats also interact with the DNA. Containing several RVDs and noncanonical associations, the structure illustrates the basis of TAL effector-DNA recognition. PubMed: 22223736DOI: 10.1126/science.1216211 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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