6OXL
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![BU of 6oxl by Molmil](/molmil-images/mine/6oxl) | CRYO-EM STRUCTURE OF PHOSPHORYLATED AP-2 (mu E302K) BOUND TO NECAP IN THE PRESENCE OF SS DNA | Descriptor: | AP-2 complex subunit alpha-2, AP-2 complex subunit beta, AP-2 complex subunit mu, ... | Authors: | Partlow, E.A, Baker, R.W, Beacham, G.M, Chappie, J, Leschziner, A.E, Hollopeter, G. | Deposit date: | 2019-05-13 | Release date: | 2019-09-11 | Last modified: | 2020-01-08 | Method: | ELECTRON MICROSCOPY (3.5 Å) | Cite: | A structural mechanism for phosphorylation-dependent inactivation of the AP2 complex. Elife, 8, 2019
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6OWO
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![BU of 6owo by Molmil](/molmil-images/mine/6owo) | CRYO-EM STRUCTURE OF PHOSPHORYLATED AP-2 CORE BOUND TO NECAP | Descriptor: | AP-2 complex subunit alpha-2, AP-2 complex subunit beta, AP-2 complex subunit mu, ... | Authors: | Partlow, E.A, Baker, R.W, Beacham, G.M, Chappie, J.S, Leschziner, A.E, Hollopeter, G. | Deposit date: | 2019-05-10 | Release date: | 2019-09-11 | Last modified: | 2020-01-08 | Method: | ELECTRON MICROSCOPY (3.2 Å) | Cite: | A structural mechanism for phosphorylation-dependent inactivation of the AP2 complex. Elife, 8, 2019
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7RW9
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![BU of 7rw9 by Molmil](/molmil-images/mine/7rw9) | AP2 bound to heparin in the bowl conformation | Descriptor: | AP-2 complex subunit alpha-2, AP-2 complex subunit beta, AP-2 complex subunit mu, ... | Authors: | Baker, R.W, Hollopeter, G, Partlow, E.A. | Deposit date: | 2021-08-19 | Release date: | 2022-03-30 | Last modified: | 2024-06-05 | Method: | ELECTRON MICROSCOPY (3.9 Å) | Cite: | Structural basis of an endocytic checkpoint that primes the AP2 clathrin adaptor for cargo internalization. Nat.Struct.Mol.Biol., 29, 2022
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7RWA
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![BU of 7rwa by Molmil](/molmil-images/mine/7rwa) | AP2 bound to heparin and Tgn38 tyrosine cargo peptide | Descriptor: | AP-2 complex subunit alpha-2, AP-2 complex subunit beta, AP-2 complex subunit mu, ... | Authors: | Baker, R.W, Hollopeter, G, Partlow, E.A. | Deposit date: | 2021-08-19 | Release date: | 2022-03-30 | Last modified: | 2024-06-05 | Method: | ELECTRON MICROSCOPY (4.7 Å) | Cite: | Structural basis of an endocytic checkpoint that primes the AP2 clathrin adaptor for cargo internalization. Nat.Struct.Mol.Biol., 29, 2022
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7RW8
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![BU of 7rw8 by Molmil](/molmil-images/mine/7rw8) | AP2 bound to heparin in the closed conformation | Descriptor: | AP-2 complex subunit alpha-2, AP-2 complex subunit beta, AP-2 complex subunit mu, ... | Authors: | Baker, R.W, Hollopeter, G, Partlow, E.A. | Deposit date: | 2021-08-19 | Release date: | 2022-03-30 | Last modified: | 2024-06-05 | Method: | ELECTRON MICROSCOPY (3.5 Å) | Cite: | Structural basis of an endocytic checkpoint that primes the AP2 clathrin adaptor for cargo internalization. Nat.Struct.Mol.Biol., 29, 2022
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7RWC
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![BU of 7rwc by Molmil](/molmil-images/mine/7rwc) | AP2 bound to the APA domain of SGIP and heparin; partial signal subtraction and symmetry expansion | Descriptor: | AP-2 complex subunit alpha-2, AP-2 complex subunit beta, AP-2 complex subunit mu, ... | Authors: | Baker, R.W, Hollopeter, G, Partlow, E.A. | Deposit date: | 2021-08-19 | Release date: | 2022-03-30 | Last modified: | 2024-06-05 | Method: | ELECTRON MICROSCOPY (3.8 Å) | Cite: | Structural basis of an endocytic checkpoint that primes the AP2 clathrin adaptor for cargo internalization. Nat.Struct.Mol.Biol., 29, 2022
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7RWB
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![BU of 7rwb by Molmil](/molmil-images/mine/7rwb) | AP2 bound to the APA domain of SGIP in the presence of heparin | Descriptor: | AP-2 complex subunit alpha-2, AP-2 complex subunit beta, AP-2 complex subunit mu, ... | Authors: | Baker, R.W, Hollopeter, G, Partlow, E.A. | Deposit date: | 2021-08-19 | Release date: | 2022-03-30 | Last modified: | 2024-06-05 | Method: | ELECTRON MICROSCOPY (3.9 Å) | Cite: | Structural basis of an endocytic checkpoint that primes the AP2 clathrin adaptor for cargo internalization. Nat.Struct.Mol.Biol., 29, 2022
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6NJX
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![BU of 6njx by Molmil](/molmil-images/mine/6njx) | C-terminal region of the Xanthomonas campestris pv. campestris OLD protein phased with mercury | Descriptor: | IODIDE ION, MERCURY (II) ION, Xcc_ctr_Hg | Authors: | Schiltz, C.J, Lee, A, Partlow, E.A, Hosford, C.J, Chappie, J.S. | Deposit date: | 2019-01-04 | Release date: | 2019-08-07 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (1.95 Å) | Cite: | Structural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavage. Nucleic Acids Res., 47, 2019
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6NK8
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![BU of 6nk8 by Molmil](/molmil-images/mine/6nk8) | C-terminal region of the Burkholderia pseudomallei OLD protein | Descriptor: | Class 2 OLD family nuclease, MAGNESIUM ION | Authors: | Schiltz, C.J, Lee, A, Partlow, E.A, Hosford, C.J, Chappie, J.S. | Deposit date: | 2019-01-05 | Release date: | 2019-08-07 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (2.24 Å) | Cite: | Structural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavage. Nucleic Acids Res., 47, 2019
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6NJW
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![BU of 6njw by Molmil](/molmil-images/mine/6njw) | C-terminal region of the Xanthomonas campestris pv. campestris OLD protein phased with platinum | Descriptor: | IODIDE ION, MAGNESIUM ION, PLATINUM (II) ION, ... | Authors: | Schiltz, C.J, Lee, A, Partlow, E.A, Hosford, C.J, Chappie, J.S. | Deposit date: | 2019-01-04 | Release date: | 2019-08-07 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (1.86 Å) | Cite: | Structural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavage. Nucleic Acids Res., 47, 2019
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6NJV
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![BU of 6njv by Molmil](/molmil-images/mine/6njv) | C-terminal region of the Xanthomonas campestris pv. campestris OLD protein phased with iodine | Descriptor: | IODIDE ION, MAGNESIUM ION, Xcc_CTR_I | Authors: | Schiltz, C.J, Lee, A, Partlow, E.A, Hosford, C.J, Chappie, J.S. | Deposit date: | 2019-01-04 | Release date: | 2019-08-07 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Structural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavage. Nucleic Acids Res., 47, 2019
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