3M6M

Crystal structure of RpfF complexed with REC domain of RpfC

Summary for 3M6M

• Entry DOI: 10.2210/pdb3m6m/pdb
• Related: 3M6N
• Descriptor: RpfF protein, Sensory/regulatory protein rpfC, IODIDE ION, ... (6 entities in total)
• Functional Keywords: rpff, rec, rpfc, enoyl-coa hydratase, lyase-transferase complex, lyase/transferase
• Biological source: Xanthomonas campestris pv. campestris; More
• Cellular location: Cell inner membrane; Multi-pass membrane protein (By similarity): P0C0F6
• Total number of polymer chains: 6
• Total formula weight: 149929.49

Authors

Cheng, Z.,Lim, S.C.,Qamra, R.,Song, H. (deposition date: 2010-03-16, release date: 2010-09-22, Last modification date: 2024-03-20)

Primary citation

Cheng, Z.,He, Y.W.,Lim, S.C.,Qamra, R.,Walsh, M.A.,Zhang, L.H.,Song, H.
Structural Basis of the Sensor-Synthase Interaction in Autoinduction of the Quorum Sensing Signal DSF Biosynthesis
Structure, 18:1199-1209, 2010

PubMed Abstract: The diffusible signal factor (DSF)-dependent quorum sensing (QS) system adopts a novel protein-protein interaction mechanism to autoregulate the production of signal DSF. Here, we present the crystal structures of DSF synthase RpfF and its complex with the REC domain of sensor protein RpfC. RpfF is structurally similarity to the members of the crotonase superfamily and contains an N-terminal α/β spiral core domain and a C-terminal α-helical region. Further structural and mutational analysis identified two catalytic glutamate residues, which is the conserved feature of the enoyl-CoA hydratases/dehydratases. A putative substrate-binding pocket was unveiled and the key roles of the residues implicated in substrate binding were verified by mutational analysis. The binding of the REC domain may lock RpfF in an inactive conformation by blocking the entrance of substrate binding pocket, thereby negatively regulating DSF production. These findings provide a structural model for the RpfC-RpfF interaction-mediated QS autoinduction mechanism.

PubMed: 20826346
DOI: 10.1016/j.str.2010.06.011

Experimental method

X-RAY DIFFRACTION (2.5 Å)