3gg1 | pdb_00003gg1

Klebsiella pneumoniae BlrP1 pH 8.0 calcium/cy-diGMP complex

spinqualitylabelsall models 3gg1, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3gg1 is a 2 chain structure with sequence from Klebsiella pneumoniae subsp. pneumoniae mgh 78578. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: C2E, CA, FMN Related: 3gfx, 3gfy, 3gfz, 3gg0 Gene: blrp1, KPN78578_15680, KPN_01598 (Klebsiella pneumoniae subsp. pneumoniae MGH 78578) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The ability to respond to light is crucial for most organisms. BLUF is a recently identified photoreceptor protein domain that senses blue light using a FAD chromophore. BLUF domains are present in various proteins from the Bacteria, Euglenozoa and Fungi. Although structures of single-domain BLUF proteins have been determined, none are available for a BLUF protein containing a functional output domain; the mechanism of light activation in this new class of photoreceptors has thus remained poorly understood. Here we report the biochemical, structural and mechanistic characterization of a full-length, active photoreceptor, BlrP1 (also known as KPN_01598), from Klebsiella pneumoniae. BlrP1 consists of a BLUF sensor domain and a phosphodiesterase EAL output domain which hydrolyses cyclic dimeric GMP (c-di-GMP). This ubiquitous second messenger controls motility, biofilm formation, virulence and antibiotic resistance in the Bacteria. Crystal structures of BlrP1 complexed with its substrate and metal ions involved in catalysis or in enzyme inhibition provide a detailed understanding of the mechanism of the EAL-domain c-di-GMP phosphodiesterases. These structures also sketch out a path of light activation of the phosphodiesterase output activity. Photon absorption by the BLUF domain of one subunit of the antiparallel BlrP1 homodimer activates the EAL domain of the second subunit through allosteric communication transmitted through conserved domain-domain interfaces. Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase.,Barends TR, Hartmann E, Griese JJ, Beitlich T, Kirienko NV, Ryjenkov DA, Reinstein J, Shoeman RL, Gomelsky M, Schlichting I Nature. 2009 Jun 18;459(7249):1015-8. PMID:19536266 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also C-di-GMP specific phosphodiesterases

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