4KKT

Crystal Structure of BesA (P21 form)

Summary for 4KKT

• Entry DOI: 10.2210/pdb4kkt/pdb
• Related: 4KKS 4KKU
• Descriptor: Membrane fusion protein (2 entities in total)
• Functional Keywords: membrane protein
• Biological source: Borrelia burgdorferi
• Total number of polymer chains: 4
• Total formula weight: 130042.67

Authors

Greene, N.P.,Hinchliffe, P.,Crow, A.,Ababou, A.,Hughes, C.,Koronakis, V. (deposition date: 2013-05-06, release date: 2013-07-10, Last modification date: 2023-09-20)

Primary citation

Greene, N.P.,Hinchliffe, P.,Crow, A.,Ababou, A.,Hughes, C.,Koronakis, V.
Structure of an atypical periplasmic adaptor from a multidrug efflux pump of the spirochete Borrelia burgdorferi.
Febs Lett., 587:2984-2988, 2013

PubMed Abstract: Periplasmic adaptor proteins are essential components of bacterial tripartite multidrug efflux pumps. Here we report the 2.35 Å resolution crystal structure of the BesA adaptor from the spirochete Borrelia burgdorferi solved using selenomethionine derivatized protein. BesA shows the archetypal linear, flexible, multi-domain architecture evident among proteobacteria and retains the lipoyl, β-barrel and membrane-proximal domains that interact with the periplasmic domains of the inner membrane transporter. However, it lacks the α-hairpin domain shown to establish extensive coiled-coil interactions with the periplasmic entrance helices of the outer membrane-anchored TolC exit duct. This has implications for the modelling of assembled tripartite efflux pumps.

PubMed: 23851070
DOI: 10.1016/j.febslet.2013.06.056

Experimental method

X-RAY DIFFRACTION (2.53 Å)