2XY8
Paramagnetic-based NMR structure of the complex between the N- terminal epsilon domain and the theta domain of the DNA polymerase III
Summary for 2XY8
| Entry DOI | 10.2210/pdb2xy8/pdb |
| Related | 1J53 1J54 1MGZ |
| Descriptor | DNA POLYMERASE III SUBUNIT EPSILON, DNA POLYMERASE III SUBUNIT THETA, CALCIUM ION (3 entities in total) |
| Functional Keywords | transferase, docking, experimental restraints, haddock program |
| Biological source | ESCHERICHIA COLI More |
| Total number of polymer chains | 2 |
| Total formula weight | 29643.07 |
| Authors | Schmitz, C.,Bonvin, A.M.J.J. (deposition date: 2010-11-16, release date: 2011-06-29, Last modification date: 2024-05-15) |
| Primary citation | Schmitz, C.,Bonvin, A.M.J.J. Protein-Protein Haddocking Using Exclusively Pseudocontact Shifts. J.Biomol.NMR, 50:263-266, 2011 Cited by PubMed Abstract: In order to enhance the structure determination process of macromolecular assemblies by NMR, we have implemented long-range pseudocontact shift (PCS) restraints into the data-driven protein docking package HADDOCK. We demonstrate the efficiency of the method on a synthetic, yet realistic case based on the lanthanide-labeled N-terminal ε domain of the E. coli DNA polymerase III (ε186) in complex with the HOT domain. Docking from the bound form of the two partners is swiftly executed (interface RMSDs < 1 Å) even with addition of very large amount of noise, while the conformational changes of the free form still present some challenges (interface RMSDs in a 3.1-3.9 Å range for the ten lowest energy complexes). Finally, using exclusively PCS as experimental information, we determine the structure of ε186 in complex with the HOT-homologue θ subunit of the E. coli DNA polymerase III. PubMed: 21626213DOI: 10.1007/S10858-011-9514-4 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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