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4i39

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(New page: '''Unreleased structure''' The entry 4i39 is ON HOLD Authors: Y.O.JUNG, J.H.LEE, J.KIM, M.SCHMIDT, S.VUKICA, K.MOFFAT, H.IHEE Description: STRUCTURES OF ICT AND PR1 INTERMEDIATES FROM ...)
Current revision (08:38, 9 November 2022) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 4i39 is ON HOLD
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==Structures of ICT and PR1 intermediates from time-resolved laue crystallography collected at 14ID-B, APS==
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<StructureSection load='4i39' size='340' side='right'caption='[[4i39]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4i39]] 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=4I39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I39 FirstGlance]. <br>
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</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4i39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i39 OCA], [https://pdbe.org/4i39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i39 RCSB], [https://www.ebi.ac.uk/pdbsum/4i39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i39 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PYP_HALHA PYP_HALHA] Photoactive blue light protein. Probably functions as a photoreceptor for a negative phototaxis response.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Y.O.JUNG, J.H.LEE, J.KIM, M.SCHMIDT, S.VUKICA, K.MOFFAT, H.IHEE
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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>
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Description: STRUCTURES OF ICT AND PR1 INTERMEDIATES FROM TIME-RESOLVED LAUE CRYSTALLOGRAPHY COLLECTED AT 14ID-B, APS
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4i39" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Halorhodospira halophila]]
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[[Category: Large Structures]]
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[[Category: Ihee H]]
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[[Category: Jung YO]]
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[[Category: Kim J]]
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[[Category: Lee JH]]
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[[Category: Moffat K]]
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[[Category: Schmidt M]]
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[[Category: Vukica S]]

Current revision

Structures of ICT and PR1 intermediates from time-resolved laue crystallography collected at 14ID-B, APS

PDB ID 4i39

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