Crystallization and preliminary X-ray data collection of the Escherichia coli lipoproteins BamC, BamD and BamE.
In Escherichia coli, the β-barrel assembly machinery (or BAM complex) mediates the recognition, insertion and assembly of outer membrane proteins. The complex consists of the integral membrane protein BamA (an Omp85-family member) and the lipoproteins BamB, BamC, BamD and BamE. The purification and crystallization of BamC, BamD and BamE, each lacking the N-terminal membrane anchor, is described. While the smallest protein BamE yielded crystals under conventional conditions, BamD only crystallized after stabilization with urea. Full-length BamC did not crystallize, but was cleaved by subtilisin into two domains which were subsequently crystallized independently. High-resolution data were acquired from all proteins.
Max-Planck-Institut für Entwicklungsbiologie, Department of Protein Evolution, Spemannstrasse 35, D-72076 Tübingen, Germany.
Reinhard
R
Albrecht
Kornelius
K
Zeth
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D058635:Lipid-Linked Proteins / Q000737:chemistry*; D008074:Lipoproteins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012645:Selenomethionine / Q000378:metabolism; D020860:Subtilisin / Q000378:metabolism
D001425:Bacterial Outer Membrane Proteins; C557407:BamB protein, E coli; C556681:BamC protein, E coli; C513739:BamD protein, E coli; C523551:BamE protein, E coli; D029968:Escherichia coli Proteins; D058635:Lipid-Linked Proteins; D008074:Lipoproteins; D012645:Selenomethionine; D020860:Subtilisin