3EFC

Crystal Structure of YaeT periplasmic domain

Summary for 3EFC

• Entry DOI: 10.2210/pdb3efc/pdb
• Descriptor: Outer membrane protein assembly factor yaeT (1 entity in total)
• Functional Keywords: potra fold, cell membrane, cell outer membrane, membrane, membrane protein
• Biological source: Escherichia coli
• Cellular location: Cell outer membrane: P0A940
• Total number of polymer chains: 1
• Total formula weight: 44187.60

Authors

Gatzeva-Topalova, P.Z.,Walton, T.A.,Sousa, M.C. (deposition date: 2008-09-08, release date: 2008-12-16, Last modification date: 2024-02-21)

Primary citation

Gatzeva-Topalova, P.Z.,Walton, T.A.,Sousa, M.C.
Crystal structure of YaeT: conformational flexibility and substrate recognition.
Structure, 16:1873-1881, 2008

PubMed Abstract: The envelope of Gram-negative bacteria consists of inner and outer membranes surrounding the peptidoglycan wall. The outer membrane (OM) is rich in integral membrane proteins (OMPs), which have a characteristic beta barrel domain embedded in the OM. The Omp85 family of proteins, ubiquitous among Gram-negative bacteria and also present in chloroplasts and mitochondria, is required for folding and insertion of OMPs into the outer membrane. Bacterial Omp85 proteins are characterized by a periplasmic domain containing five repeats of polypeptide transport-associated (POTRA) motifs. Here we report the crystal structure of a periplasmic fragment of YaeT (the Escherichia coli Omp85) containing the first four POTRA domains in an extended conformation consistent with recent solution X-ray scattering data. Analysis of the YaeT structure reveals conformational flexibility around a hinge point between POTRA2 and 3 domains. The structure's implications for substrate binding and folding mechanisms are also discussed.

PubMed: 19081063
DOI: 10.1016/j.str.2008.09.014

Experimental method

X-RAY DIFFRACTION (3.3 Å)