2QDF
Structure of N-terminal domain of E. Coli YaeT
Summary for 2QDF
| Entry DOI | 10.2210/pdb2qdf/pdb |
| Related | 2QCZ |
| Descriptor | Outer membrane protein assembly factor yaeT, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | potra domain, membrane protein, protein transport |
| Biological source | Escherichia coli K12 |
| Cellular location | Cell outer membrane : P0A940 |
| Total number of polymer chains | 1 |
| Total formula weight | 37479.47 |
| Authors | Kim, S.,Malinverni, J.C.,Sliz, P.,Silhavy, T.J.,Harrison, S.C.,Kahne, D. (deposition date: 2007-06-20, release date: 2007-09-04, Last modification date: 2023-08-30) |
| Primary citation | Kim, S.,Malinverni, J.C.,Sliz, P.,Silhavy, T.J.,Harrison, S.C.,Kahne, D. Structure and function of an essential component of the outer membrane protein assembly machine. Science, 317:961-964, 2007 Cited by PubMed Abstract: Integral beta-barrel proteins are found in the outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria. The machine that assembles these proteins contains an integral membrane protein, called YaeT in Escherichia coli, which has one or more polypeptide transport-associated (POTRA) domains. The crystal structure of a periplasmic fragment of YaeT reveals the POTRA domain fold and suggests a model for how POTRA domains can bind different peptide sequences, as required for a machine that handles numerous beta-barrel protein precursors. Analysis of POTRA domain deletions shows which are essential and provides a view of the spatial organization of this assembly machine. PubMed: 17702946DOI: 10.1126/science.1143993 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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