4i3a: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4i3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i3a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i3a RCSB], [http://www.ebi.ac.uk/pdbsum/4i3a PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4i3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i3a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i3a RCSB], [http://www.ebi.ac.uk/pdbsum/4i3a PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://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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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 13:45, 25 December 2014
Structures of PR1 and PR2 intermediates from time-resolved laue crystallography collected at 14ID-B, APSStructures of PR1 and PR2 intermediates from time-resolved laue crystallography collected at 14ID-B, APS
Structural highlights
Function[PYP_HALHA] Photoactive blue light protein. Probably functions as a photoreceptor for a negative phototaxis response. Publication Abstract from PubMedTrans-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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