View source for 5mbe


==Structure of a bacterial light-regulated adenylyl cylcase==
<StructureSection load='5mbe' size='340' side='right'caption='[[5mbe]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mbe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Beggiatoa_sp._PS Beggiatoa sp. PS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MBE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></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=5mbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mbe OCA], [https://pdbe.org/5mbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mbe RCSB], [https://www.ebi.ac.uk/pdbsum/5mbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mbe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A7BT71_9GAMM A7BT71_9GAMM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Light-regulated enzymes enable organisms to quickly respond to changing light conditions. We characterize a photoactivatable adenylyl cyclase from Beggiatoa sp. (bPAC) that translates a blue light signal into production of the second messenger cyclic AMP. bPAC contains a BLUF photoreceptor domain that senses blue light using a flavin chromophore, linked to an adenylyl cyclase (AC) domain. We present a dark state crystal structure of bPAC that closely resembles the recently published structure of the homologous OaPAC from Oscillatoria acuminata. To elucidate the structural mechanism of light-dependent AC activation by the BLUF domain, we determined crystal structures of illuminated bPAC and of a pseudo-lit state variant. We use hydrogen-deuterium exchange measurements of secondary structure dynamics and hypothesis-driven point mutations to trace the activation pathway from the chromophore in the BLUF domain to the active site of the cyclase. The structural changes are relayed from the residues interacting with the excited chromophore through a conserved kink of the BLUF beta-sheet to a tongue-like extrusion of the AC domain that regulates active site opening and repositions catalytic residues. Our findings not only show the specific molecular pathway of photoactivation in BLUF-regulated ACs, but they also have implications for the general understanding of signaling in BLUF domains and of the activation of adenylyl cyclases.

Photoactivation mechanism of a bacterial light-regulated adenylyl cyclase.,Lindner R, Hartmann E, Tarnawski M, Winkler A, Frey D, Reinstein J, Meinhart A, Schlichting I J Mol Biol. 2017 Mar 20. pii: S0022-2836(17)30124-9. doi:, 10.1016/j.jmb.2017.03.020. PMID:28336405<ref>PMID:28336405</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5mbe" style="background-color:#fffaf0;"></div>

==See Also==
*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Beggiatoa sp. PS]]
[[Category: Large Structures]]
[[Category: Frey D]]
[[Category: Hartmann E]]
[[Category: Lindner R]]
[[Category: Meinhart A]]
[[Category: Reinstein J]]
[[Category: Schlichting I]]
[[Category: Tarnawski M]]
[[Category: Winkler A]]