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<StructureSection load='3gg0' size='340' side='right'caption='[[3gg0]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
<StructureSection load='3gg0' size='340' side='right'caption='[[3gg0]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3gg0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Klep7 Klep7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GG0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3gg0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae_subsp._pneumoniae_MGH_78578 Klebsiella pneumoniae subsp. pneumoniae MGH 78578]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GG0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2E: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)'>C2E</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3gfx|3gfx]], [[3gfy|3gfy]], [[3gfz|3gfz]], [[3gg1|3gg1]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2E: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)'>C2E</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blrp, KPN78578_15680, KPN_01598 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272620 KLEP7])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gg0 OCA], [https://pdbe.org/3gg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gg0 RCSB], [https://www.ebi.ac.uk/pdbsum/3gg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gg0 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gg0 OCA], [https://pdbe.org/3gg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gg0 RCSB], [https://www.ebi.ac.uk/pdbsum/3gg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gg0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A6T8V8_KLEP7 A6T8V8_KLEP7]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3gg0 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3gg0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:19536266</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3gg0" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[C-di-GMP specific phosphodiesterases|C-di-GMP specific phosphodiesterases]]
*[[C-di-GMP specific phosphodiesterases|C-di-GMP specific phosphodiesterases]]
*[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]]
*[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Klep7]]
[[Category: Klebsiella pneumoniae subsp. pneumoniae MGH 78578]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Barends, T]]
[[Category: Barends T]]
[[Category: Beitlich, T]]
[[Category: Beitlich T]]
[[Category: Gomelsky, M]]
[[Category: Gomelsky M]]
[[Category: Griese, J]]
[[Category: Griese J]]
[[Category: Hartmann, E]]
[[Category: Hartmann E]]
[[Category: Kirienko, N]]
[[Category: Kirienko N]]
[[Category: Reinstein, J]]
[[Category: Reinstein J]]
[[Category: Ryjenkov, D]]
[[Category: Ryjenkov D]]
[[Category: Schlichting, I]]
[[Category: Schlichting I]]
[[Category: Shoeman, R]]
[[Category: Shoeman R]]
[[Category: Bluf domain]]
[[Category: Eal domain]]
[[Category: Hydrolase]]
[[Category: Signaling protein]]
[[Category: Tim-barrel]]

Latest revision as of 09:54, 21 February 2024

Klebsiella pneumoniae BlrP1 pH 9.0 manganese/cy-diGMP complex

3gg0, resolution 2.55Å

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