4ETX

Crystal Structure of PelD 158-CT from Pseudomonas aeruginosa PAO1

Summary for 4ETX

• Entry DOI: 10.2210/pdb4etx/pdb
• Related: 4ETZ 4EU0
• Descriptor: PelD (2 entities in total)
• Functional Keywords: c-di-gmp, signaling protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 33712.34

Authors

Li, Z.,Chen, J.,Nair, S.K. (deposition date: 2012-04-24, release date: 2012-07-25, Last modification date: 2024-02-28)

Primary citation

Li, Z.,Chen, J.H.,Hao, Y.,Nair, S.K.
Structures of the PelD Cyclic Diguanylate Effector Involved in Pellicle Formation in Pseudomonas aeruginosa PAO1.
J.Biol.Chem., 287:30191-30204, 2012

PubMed Abstract: The second messenger bis-(3'-5')-cyclic dimeric guanosine monophosphate (c-di-GMP) plays a vital role in the global regulation in bacteria. Here, we describe structural and biochemical characterization of a novel c-di-GMP effector PelD that is critical to the formation of pellicles by Pseudomonas aeruginosa. We present high-resolution structures of a cytosolic fragment of PelD in apo form and its complex with c-di-GMP. The structure contains a bi-domain architecture composed of a GAF domain (commonly found in cyclic nucleotide receptors) and a GGDEF domain (found in c-di-GMP synthesizing enzymes), with the latter binding to one molecule of c-di-GMP. The GGDEF domain has a degenerate active site but a conserved allosteric site (I-site), which we show binds c-di-GMP with a K(d) of 0.5 μm. We identified a series of residues that are crucial for c-di-GMP binding, and confirmed the roles of these residues through biochemical characterization of site-specific variants. The structures of PelD represent a novel class of c-di-GMP effector and expand the knowledge of scaffolds that mediate c-di-GMP recognition.

PubMed: 22810222
DOI: 10.1074/jbc.M112.378273

Experimental method

X-RAY DIFFRACTION (2 Å)