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M (2009) the peptidoglycan-binding (pgb) domain of the escherichia coli pal protein can also function as the pgb domain in e. Coli flagellar motor protein motb. J biochem 146: 219–229. Accession codes coordinates and structure factors have been deposited.
| Content Provider | CiteSeerX |
|---|---|
| Author | Hizukuri, Yohei Morton, John Frederick Yakushi, Toshiharu Kojima, Seiji Hommay, Michio |
| Abstract | The bacterial flagellar stator proteins, MotA and MotB, form a complex and are thought to be anchored to the peptidoglycan by the C-terminal conserved peptido-glycan-binding (PGB) motif of MotB. To clarify the role of the C-terminal region, we performed systematic cysteine mutagenesis and constructed a chimeric MotB protein which was replaced with the peptidoglycan-associated lipoprotein Pal. Although this chimera could not restore motility to a motB strain, we were able to isolate two motile revertants. One was F172V in the Pal region and the other was P159L in the MotB region. Furthermore, we attempted to map the MotB Cys muta-tions in the crystal structure of Escherichia coli Pal. We found that the MotB muta-tions that affected motility nearly overlapped with the predicted PG-binding residues of Pal. Our results indicate that, although the functions of MotB and Pal are very different, the PGB region of Pal is interchangeable with the PGB region of MotB. |
| File Format | |
| Access Restriction | Open |
| Subject Keyword | Structure Factor Pgb Domain Flagellar Motor Protein Motb Escherichia Coli Pal Protein Pgb Region Motile Revertants Crystal Structure Motb Cys Muta-tions C-terminal Region Predicted Pg-binding Residue Motb Region Motb Muta-tions Peptidoglycan-associated Lipoprotein Pal Escherichia Coli Pal Chimeric Motb Protein Bacterial Flagellar Stator Protein Motb Strain C-terminal Conserved Peptido-glycan-binding Systematic Cysteine Mutagenesis Pal Region |
| Content Type | Text |
