3ve4: Difference between revisions
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New page: '''Unreleased structure''' The entry 3ve4 is ON HOLD Authors: Ihee, H., Jung, Y.O. Description: STRUCTURES OF ICT AND PR1 INTERMEDIATES FROM TIME-RESOLVED LAUE CRYSTALLOGRAPHY |
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The | ==Structures of ICT and PR1 intermediates from time-resolved laue crystallography== | ||
<StructureSection load='3ve4' size='340' side='right'caption='[[3ve4]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ve4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halorhodospira_halophila Halorhodospira halophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VE4 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]] 1.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HC4:4-HYDROXYCINNAMIC+ACID'>HC4</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=3ve4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ve4 OCA], [https://pdbe.org/3ve4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ve4 RCSB], [https://www.ebi.ac.uk/pdbsum/3ve4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ve4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PYP_HALHA PYP_HALHA] Photoactive blue light protein. Probably functions as a photoreceptor for a negative phototaxis response. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Trans-to-cis isomerization, the key reaction in photoactive proteins, usually cannot occur through the standard one-bond-flip mechanism. Owing to spatial constraints imposed by a protein environment, isomerization probably proceeds through a volume-conserving mechanism in which highly choreographed atomic motions are expected, the details of which have not yet been observed directly. Here we employ time-resolved X-ray crystallography to visualize structurally the isomerization of the p-coumaric acid chromophore in photoactive yellow protein with a time resolution of 100 ps and a spatial resolution of 1.6 A. The structure of the earliest intermediate (I(T)) resembles a highly strained transition state in which the torsion angle is located halfway between the trans- and cis-isomers. The reaction trajectory of I(T) bifurcates into two structurally distinct cis intermediates via hula-twist and bicycle-pedal pathways. The bifurcating reaction pathways can be controlled by weakening the hydrogen bond between the chromophore and an adjacent residue through E46Q mutation, which switches off the bicycle-pedal pathway. | |||
Volume-conserving trans-cis isomerization pathways in photoactive yellow protein visualized by picosecond X-ray crystallography.,Jung YO, Lee JH, Kim J, Schmidt M, Moffat K, Srajer V, Ihee H Nat Chem. 2013 Mar;5(3):212-20. doi: 10.1038/nchem.1565. Epub 2013 Feb 3. PMID:23422563<ref>PMID:23422563</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3ve4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Halorhodospira halophila]] | |||
[[Category: Large Structures]] | |||
[[Category: Ihee H]] | |||
[[Category: Jung YO]] | |||
Latest revision as of 22:50, 26 March 2025
Structures of ICT and PR1 intermediates from time-resolved laue crystallography
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