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| | <StructureSection load='5x4u' size='340' side='right'caption='[[5x4u]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='5x4u' size='340' side='right'caption='[[5x4u]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5x4u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/9cyan 9cyan]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X4U OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5X4U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5x4u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyanobacteria Cyanobacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X4U FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x4t|5x4t]], [[5x4v|5x4v]]</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'>[http://proteopedia.org/fgij/fg.htm?mol=5x4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x4u OCA], [http://pdbe.org/5x4u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x4u RCSB], [http://www.ebi.ac.uk/pdbsum/5x4u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x4u 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=5x4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x4u OCA], [https://pdbe.org/5x4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x4u RCSB], [https://www.ebi.ac.uk/pdbsum/5x4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x4u ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/K9TLZ5_9CYAN K9TLZ5_9CYAN] |
| - | The photoactivated adenylate cyclase (PAC) from the photosynthetic cyanobacterium Oscillatoria acuminata (OaPAC) detects light through a flavin chromophore within the N-terminal BLUF domain. BLUF domains have been found in a number of different light-activated proteins, but with different relative orientations. The two BLUF domains of OaPAC are found in close contact with each other, forming a coiled coil at their interface. Crystallization does not impede the activity switching of the enzyme, but flash cooling the crystals to cryogenic temperatures prevents the signature spectral changes that occur on photoactivation/deactivation. High-resolution crystallographic analysis of OaPAC in the fully activated state has been achieved by cryocooling the crystals immediately after light exposure. Comparison of the isomorphous light- and dark-state structures shows that the active site undergoes minimal changes, yet enzyme activity may increase up to 50-fold, depending on conditions. The OaPAC models will assist the development of simple, direct means to raise the cyclic AMP levels of living cells by light, and other tools for optogenetics.
| + | |
| - | | + | |
| - | Molecular mechanism of photoactivation of a light-regulated adenylate cyclase.,Ohki M, Sato-Tomita A, Matsunaga S, Iseki M, Tame JRH, Shibayama N, Park SY Proc Natl Acad Sci U S A. 2017 Aug 8;114(32):8562-8567. doi:, 10.1073/pnas.1704391114. Epub 2017 Jul 24. PMID:28739908<ref>PMID:28739908</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5x4u" style="background-color:#fffaf0;"></div>
| + | |
| | | | |
| | ==See Also== | | ==See Also== |
| | *[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]] | | *[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Cyanobacteria]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ohki, M]] | + | [[Category: Ohki M]] |
| - | [[Category: Park, S Y]] | + | [[Category: Park S-Y]] |
| - | [[Category: Allostery]]
| + | |
| - | [[Category: Bluf domain]]
| + | |
| - | [[Category: Camp]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Optogenetic]]
| + | |
| - | [[Category: Photoactivation]]
| + | |
