3GG0

Klebsiella pneumoniae BlrP1 pH 9.0 manganese/cy-diGMP complex

Summary for 3GG0

• Entry DOI: 10.2210/pdb3gg0/pdb
• Related: 3GFX 3GFY 3GFZ 3GG1
• Descriptor: Klebsiella pneumoniae BlrP1, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one), MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: tim-barrel, eal domain, bluf domain, hydrolase, signaling protein
• Biological source: Klebsiella pneumoniae subsp. pneumoniae MGH 78578
• Total number of polymer chains: 2
• Total formula weight: 94382.93

Authors

Barends, T.,Hartmann, E.,Griese, J.,Beitlich, T.,Kirienko, N.,Ryjenkov, D.,Reinstein, J.,Shoeman, R.,Gomelsky, M.,Schlichting, I. (deposition date: 2009-02-27, release date: 2009-06-23, Last modification date: 2024-02-21)

Primary citation

Barends, T.R.,Hartmann, E.,Griese, J.J.,Beitlich, T.,Kirienko, N.V.,Ryjenkov, D.A.,Reinstein, J.,Shoeman, R.L.,Gomelsky, M.,Schlichting, I.
Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase.
Nature, 459:1015-1018, 2009

PubMed Abstract: 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.

PubMed: 19536266
DOI: 10.1038/nature07966

Experimental method

X-RAY DIFFRACTION (2.55 Å)