2QCZ

Structure of N-terminal domain of E. Coli YaeT

Summary for 2QCZ

• Entry DOI: 10.2210/pdb2qcz/pdb
• Descriptor: Outer membrane protein assembly factor yaeT (1 entity 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: 2
• Total formula weight: 74910.34

Authors

Kim, S.,Malinverni, J.C.,Sliz, P.,Silhavy, T.J.,Harrison, S.C.,Kahne, D. (deposition date: 2007-06-20, release date: 2007-08-28, Last modification date: 2024-02-21)

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

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: 17702946
DOI: 10.1126/science.1143993

Experimental method

X-RAY DIFFRACTION (2.7 Å)