2LUM
Three-State Ensemble obtained from eNOEs of the Third Immunoglobulin Binding Domain of Protein G (GB3)
Summary for 2LUM
| Entry DOI | 10.2210/pdb2lum/pdb |
| Related | 1IGD 1P7E 1P7F 2OED |
| NMR Information | BMRB: 18531 |
| Descriptor | Immunoglobulin G-binding protein G (1 entity in total) |
| Functional Keywords | correlated dynamics, noe, enoe, exact nuclear overhauser effect, structure calculation, structure ensemble, protein binding |
| Biological source | Streptococcus sp. 'group G' |
| Cellular location | Secreted, cell wall; Peptidoglycan-anchor (Potential): P19909 |
| Total number of polymer chains | 1 |
| Total formula weight | 6214.85 |
| Authors | Vogeli, B.,Kazemi, S.,Guntert, P.,Riek, R. (deposition date: 2012-06-18, release date: 2012-08-29, Last modification date: 2024-05-15) |
| Primary citation | Vogeli, B.,Kazemi, S.,Guntert, P.,Riek, R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs. Nat.Struct.Mol.Biol., 19:1053-1057, 2012 Cited by PubMed Abstract: Proteins are inherently dynamic systems whose motions cover large ranges in both magnitude and timescale. Because of the omnipresence of motion, it is likely that dynamics have important roles in the function of biomolecules. For detailed understanding of a protein's function, the three-dimensional structure and description of its dynamics are therefore required. Structure determination methods are well established, and NMR-relaxation phenomena provide insights into local molecular dynamics; moreover, recently several attempts have been made to detect concerted motion. Here, we present an ensemble-based structure-determination protocol using ensemble-averaged distance restraints obtained from exact NOE rates. Application to the model protein GB3 establishes an ensemble of structures that reveals correlated motion across the β-sheet, concerted motion between the backbone and side chains localized in the structure core, and a lack of concerted conformational exchange between the β-sheet and the α-helix. PubMed: 22940676DOI: 10.1038/nsmb.2355 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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