1ba3: Difference between revisions
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<StructureSection load='1ba3' size='340' side='right'caption='[[1ba3]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1ba3' size='340' side='right'caption='[[1ba3]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ba3]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ba3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Common_eastern_firefly Common eastern firefly]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BA3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BA3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MBR:TRIBROMOMETHANE'>MBR</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MBR:TRIBROMOMETHANE'>MBR</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Photinus-luciferin_4-monooxygenase_(ATP-hydrolyzing) Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.7 1.13.12.7] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ba3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ba3 OCA], [https://pdbe.org/1ba3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ba3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ba3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ba3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/LUCI_PHOPY LUCI_PHOPY]] Produces green light with a wavelength of 562 nm. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Luciferase|Luciferase]] | *[[Luciferase 3D structures|Luciferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 18:05, 2 June 2021
FIREFLY LUCIFERASE IN COMPLEX WITH BROMOFORMFIREFLY LUCIFERASE IN COMPLEX WITH BROMOFORM
Structural highlights
Function[LUCI_PHOPY] Produces green light with a wavelength of 562 nm. 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 PubMedThe firefly luciferase enzyme from Photinus pyralis is probably the best-characterized model system for studying anesthetic-protein interactions. It binds a diverse range of general anesthetics over a large potency range, displays a sensitivity to anesthetics that is very similar to that found in animals, and has an anesthetic sensitivity that can be modulated by one of its substrates (ATP). In this paper we describe the properties of bromoform acting as a general anesthetic (in Rana temporaria tadpoles) and as an inhibitor of the firefly luciferase enzyme at high and low ATP concentrations. In addition, we describe the crystal structure of the low-ATP form of the luciferase enzyme in the presence of bromoform at 2.2-A resolution. These results provide a structural basis for understanding the anesthetic inhibition of the enzyme, as well as an explanation for the ATP modulation of its anesthetic sensitivity. Structural basis for the inhibition of firefly luciferase by a general anesthetic.,Franks NP, Jenkins A, Conti E, Lieb WR, Brick P Biophys J. 1998 Nov;75(5):2205-11. PMID:9788915[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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