2zoi: Difference between revisions

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New page: '''Unreleased structure''' The entry 2zoi is ON HOLD until May 21 2010 Authors: Yamaguchi, S., Kamikubo, H., Kurihara, K., Kuroki, R., Niimura, N., Shimizu, N., Yamazaki, Y., Kataoka, M...
 
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'''Unreleased structure'''


The entry 2zoi is ON HOLD  until May 21 2010
==Neutron Crystal Structure of Photoactive Yellow Protein, Wild type, at 295K==
<StructureSection load='2zoi' size='340' side='right'caption='[[2zoi]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2zoi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halorhodospira_halophila Halorhodospira halophila]. The March 2015 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Phototropin''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2015_3 10.2210/rcsb_pdb/mom_2015_3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZOI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Neutron Diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <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=2zoi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zoi OCA], [https://pdbe.org/2zoi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zoi RCSB], [https://www.ebi.ac.uk/pdbsum/2zoi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zoi 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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <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>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2zoi ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Low-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.


Authors: Yamaguchi, S., Kamikubo, H., Kurihara, K., Kuroki, R., Niimura, N., Shimizu, N., Yamazaki, Y., Kataoka, M.
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<ref>PMID:19122140</ref>


Description: Neutron Crystal Structure of Photoactive Yellow Protein, Wild type, at 295K
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
 
<div class="pdbe-citations 2zoi" style="background-color:#fffaf0;"></div>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 09:23:31 2008''
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Halorhodospira halophila]]
[[Category: Large Structures]]
[[Category: Phototropin]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Yamaguchi S]]

Latest revision as of 13:46, 1 November 2023

Neutron Crystal Structure of Photoactive Yellow Protein, Wild type, at 295K

2zoi, resolution 1.50Å

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