Structure of TAL effector PthXo1 bound to its DNA target. Determined by X-ray diffraction at 3.0 Å resolution. Released 4 Jan 2012.
Explore 3UGM in 3D Show helices and sheets RCSB PDB PDBe
3UGM contains 58 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 222-228 | 7 | |
| α-helix | 234-245 | 12 | |
| α-helix | 258-266 | 9 | |
| α-helix | 268-282 | 15 | |
| α-helix | 291-298 | 8 | |
| α-helix | 303-313 | 11 | |
| α-helix | 315-319 | 5 | |
| α-helix | 325-328 | 4 | |
| α-helix | 337-354 | 18 | |
| α-helix | 359-366 | 8 | |
| α-helix | 371-381 | 11 | |
| α-helix | 383-389 | 7 | |
| α-helix | 393-400 | 8 | |
| α-helix | 405-422 | 18 | |
| α-helix | 427-434 | 8 | |
| α-helix | 440-454 | 15 | |
| α-helix | 461-468 | 8 | |
| α-helix | 473-488 | 16 | |
| α-helix | 495-504 | 10 | |
| α-helix | 506-521 | 16 | |
| α-helix | 528-535 | 8 | |
| α-helix | 541-552 | 12 | |
| α-helix | 553-557 | 5 | |
| α-helix | 562-568 | 7 | |
| α-helix | 574-591 | 18 | |
| α-helix | 597-603 | 7 | |
| α-helix | 608-618 | 11 | |
| α-helix | 620-622 | 3 | |
| α-helix | 631-637 | 7 | |
| α-helix | 643-656 | 14 | |
| α-helix | 664-670 | 7 | |
| α-helix | 676-686 | 11 | |
| α-helix | 688-694 | 7 | |
| α-helix | 699-702 | 4 | |
| α-helix | 711-727 | 17 | |
| α-helix | 733-739 | 7 | |
| α-helix | 744-754 | 11 | |
| α-helix | 757-760 | 4 | |
| α-helix | 766-769 | 4 | |
| α-helix | 778-788 | 11 | |
| α-helix | 800-807 | 8 | |
| α-helix | 812-826 | 15 | |
| α-helix | 835-841 | 7 | |
| α-helix | 846-854 | 9 | |
| α-helix | 868-875 | 8 | |
| α-helix | 880-893 | 14 | |
| α-helix | 894-898 | 5 | |
| α-helix | 902-909 | 8 | |
| α-helix | 914-929 | 16 | |
| α-helix | 936-943 | 8 | |
| α-helix | 948-958 | 11 | |
| α-helix | 960-964 | 5 | |
| α-helix | 970-976 | 7 | |
| α-helix | 985-993 | 9 | |
| α-helix | 994-1000 | 7 | |
| α-helix | 1004-1011 | 8 | |
| α-helix | 1015-1023 | 9 | |
| α-helix | 1026-1031 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| TAL effector AvrBs3/PthA | A | protein | 1047 | Xanthomonas oryzae | B2SU53 (AlphaFold model) |
| DNA-1 | B | DNA | 38 | ||
| DNA-2 | C | DNA | 38 |
>3UGM_1 TAL effector AvrBs3/PthA (chains A) MASSHHHHHHSSGLVPRGSSGSSMAARPPRAKPAPRRRAAQPSDASPAAQVDLRTLGYSQ QQQEKIKPKVRSTVAQHHEALVGHGFTHAHIVALSQHPAALGTVAVTYQHIITALPEATH EDIVGVGKQWSGARALEALLTDAGELRGPPLQLDTGQLVKIAKRGGVTAMEAVHASRNAL TGAPLNLTPAQVVAIASNNGGKQALETVQRLLPVLCQAHGLTPAQVVAIASHDGGKQALE TMQRLLPVLCQAHGLPPDQVVAIASNIGGKQALETVQRLLPVLCQAHGLTPDQVVAIASH GGGKQALETVQRLLPVLCQAHGLTPDQVVAIASHDGGKQALETVQRLLPVLCQAHGLTPD QVVAIASNGGGKQALETVQRLLPVLCQAHGLTPDQVVAIASNGGKQALETVQRLLPVLCQ AHGLTPDQVVAIASHDGGKQALETVQRLLPVLCQTHGLTPAQVVAIASHDGGKQALETVQ QLLPVLCQAHGLTPDQVVAIASNIGGKQALATVQRLLPVLCQAHGLTPDQVVAIASNGGG KQALETVQRLLPVLCQAHGLTPDQVVAIASNGGGKQALETVQRLLPVLCQAHGLTQVQVV AIASNIGGKQALETVQRLLPVLCQAHGLTPAQVVAIASHDGGKQALETVQRLLPVLCQAH GLTPDQVVAIASNGGGKQALETVQRLLPVLCQAHGLTQEQVVAIASNNGGKQALETVQRL LPVLCQAHGLTPDQVVAIASNGGGKQALETVQRLLPVLCQAHGLTPAQVVAIASNIGGKQ ALETVQRLLPVLCQDHGLTLAQVVAIASNIGGKQALETVQRLLPVLCQAHGLTQDQVVAI ASNIGGKQALETVQRLLPVLCQDHGLTPDQVVAIASNIGGKQALETVQRLLPVLCQDHGL TLDQVVAIASNGGKQALETVQRLLPVLCQDHGLTPDQVVAIASNSGGKQALETVQRLLPV LCQDHGLTPNQVVAIASNGGKQALESIVAQLSRPDPALAALTNDHLVALACLGGRPAMDA VKKGLPHAPELIRRVNRRIGERTSHRV
>3UGM_2 DNA-1 (chains B) TAGATATGCATCTCCCCCTACTGTACACCACCAAAAGT
>3UGM_3 DNA-2 (chains C) TTTTGGTGGTGTACAGTAGGGGGAGATGCATATCTAAC
The Crystal Structure of TAL Effector PthXo1 Bound to Its DNA Target. Mak, A.N., Bradley, P., Cernadas, R.A. et al. Science (2012) 335:716-719. DOI 10.1126/science.1216211 · PubMed
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