3qyy | pdb_00003qyy

A Novel Interaction Mode between a Microbial GGDEF Domain and the Bis-(3, 5 )-cyclic di-GMP

spinqualitylabelsall models 3qyy, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qyy is a 2 chain structure with sequence from Xanthomonas campestris pv. campestris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: C2E, MG, PEG Gene: XCC3486 (Xanthomonas campestris pv. campestris) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Cyclic diguanosine monophosphate (c-di-GMP) is a key signalling molecule involved in regulating many important biological functions in bacteria. The synthesis of c-di-GMP is catalyzed by the GGDEF-domain-containing diguanylate cyclase (DGC), the activity of which is regulated by the binding of product at the allosteric inhibitory (I) site. However, a significant number of GGDEF domains lack the RxxD motif characteristic of the allosteric I site. Here, the structure of XCC4471(GGDEF), the GGDEF domain of a DGC from Xanthomonas campestris, in complex with c-di-GMP has been solved. Unexpectedly, the structure of the complex revealed a GGDEF-domain dimer cross-linked by two molecules of c-di-GMP at the strongly conserved active sites. In the complex (c-di-GMP)(2) adopts a novel partially intercalated form, with the peripheral guanine bases bound to the guanine-binding pockets and the two central bases stacked upon each other. Alteration of the residues involved in specific binding to c-di-GMP led to dramatically reduced K(d) values between XCC4471(GGDEF) and c-di-GMP. In addition, these key residues are strongly conserved among the many thousands of GGDEF-domain sequences identified to date. These results indicate a new product-bound form for GGDEF-domain-containing proteins obtained via (c-di-GMP)(2) binding at the active site. This novel XCC4471(GGDEF)-c-di-GMP complex structure may serve as a general model for the design of lead compounds to block the DGC activity of GGDEF-domain-containing proteins in X. campestris or other microorganisms that contain multiple GGDEF-domain proteins. The structure and inhibition of a GGDEF diguanylate cyclase complexed with (c-di-GMP)(2) at the active site.,Yang CY, Chin KH, Chuah ML, Liang ZX, Wang AH, Chou SH Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):997-1008. Epub 2011 Nov, 18. PMID:22120736 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Response regulator

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