2zoi: Difference between revisions
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==Neutron Crystal Structure of Photoactive Yellow Protein, Wild type, at 295K== | ==Neutron Crystal Structure of Photoactive Yellow Protein, Wild type, at 295K== | ||
<StructureSection load='2zoi' size='340' side='right' caption='[[2zoi]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='2zoi' size='340' side='right' caption='[[2zoi]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zoh|2zoh]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zoh|2zoh]]</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=2zoi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zoi OCA], [http://pdbe.org/2zoi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zoi RCSB], [http://www.ebi.ac.uk/pdbsum/2zoi 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=2zoi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zoi OCA], [http://pdbe.org/2zoi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zoi RCSB], [http://www.ebi.ac.uk/pdbsum/2zoi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zoi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zo/2zoi_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zo/2zoi_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 08:38, 8 March 2018
Neutron Crystal Structure of Photoactive Yellow Protein, Wild type, at 295KNeutron Crystal Structure of Photoactive Yellow Protein, Wild type, at 295K
Structural highlights
Function[PYP_HALHA] Photoactive blue light protein. Probably functions as a photoreceptor for a negative phototaxis response. 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 PubMedLow-barrier hydrogen bonds (LBHBs) have been proposed to play roles in protein functions, including enzymatic catalysis and proton transfer. Transient formation of LBHBs is expected to stabilize specific reaction intermediates. However, based on experimental results and theoretical considerations, arguments against the importance of LBHB in proteins have been raised. The discrepancy is caused by the absence of direct identification of the hydrogen atom position. Here, we show by high-resolution neutron crystallography of photoactive yellow protein (PYP) that a LBHB exists in a protein, even in the ground state. We identified approximately 87% (819/942) of the hydrogen positions in PYP and demonstrated that the hydrogen bond between the chromophore and E46 is a LBHB. This LBHB stabilizes an isolated electric charge buried in the hydrophobic environment of the protein interior. We propose that in the excited state the fast relaxation of the LBHB into a normal hydrogen bond is the trigger for photo-signal propagation to the protein moiety. These results give insights into the novel roles of LBHBs and the mechanism of the formation of LBHBs. Low-barrier hydrogen bond in photoactive yellow protein.,Yamaguchi S, Kamikubo H, Kurihara K, Kuroki R, Niimura N, Shimizu N, Yamazaki Y, Kataoka M Proc Natl Acad Sci U S A. 2009 Jan 13;106(2):440-4. Epub 2009 Jan 2. PMID:19122140[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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