4i3a: Difference between revisions
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==Structures of PR1 and PR2 intermediates from time-resolved laue crystallography collected at 14ID-B, APS== | ==Structures of PR1 and PR2 intermediates from time-resolved laue crystallography collected at 14ID-B, APS== | ||
<StructureSection load='4i3a' size='340' side='right' caption='[[4i3a]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='4i3a' size='340' side='right' caption='[[4i3a]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hy8|4hy8]], [[4i38|4i38]], [[4i39|4i39]], [[4i3i|4i3i]], [[4i3j|4i3j]], [[3ve3|3ve3]], [[3ve4|3ve4]], [[1ts0|1ts0]], [[1ts6|1ts6]], [[1ts7|1ts7]], [[1ts8|1ts8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hy8|4hy8]], [[4i38|4i38]], [[4i39|4i39]], [[4i3i|4i3i]], [[4i3j|4i3j]], [[3ve3|3ve3]], [[3ve4|3ve4]], [[1ts0|1ts0]], [[1ts6|1ts6]], [[1ts7|1ts7]], [[1ts8|1ts8]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pyp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1053 DSM 244])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pyp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1053 DSM 244])</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> | <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://pdbe.org/4i3a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i3a RCSB], [http://www.ebi.ac.uk/pdbsum/4i3a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i3a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4i3a" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 18:54, 4 August 2016
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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