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==CRYOTRAPPED STATE IN WILD TYPE PHOTOACTIVE YELLOW PROTEIN, INDUCED WITH CONTINUOUS ILLUMINATION AT 110K==
==CRYOTRAPPED STATE IN WILD TYPE PHOTOACTIVE YELLOW PROTEIN, INDUCED WITH CONTINUOUS ILLUMINATION AT 110K==
<StructureSection load='1ot9' size='340' side='right' caption='[[1ot9]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
<StructureSection load='1ot9' size='340' side='right'caption='[[1ot9]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ot9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_244 Dsm 244]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OT9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OT9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ot9]] 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=1OT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OT9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HC4:4-HYDROXYCINNAMIC+ACID'>HC4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ot6|1ot6]], [[1ota|1ota]], [[1otb|1otb]], [[1ot1|1ot1]], [[1ote|1ote]], [[1otd|1otd]]</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>
<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'>[https://proteopedia.org/fgij/fg.htm?mol=1ot9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ot9 OCA], [https://pdbe.org/1ot9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ot9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ot9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ot9 ProSAT]</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=1ot9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ot9 OCA], [http://pdbe.org/1ot9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ot9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ot9 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PYP_HALHA PYP_HALHA]] Photoactive blue light protein. Probably functions as a photoreceptor for a negative phototaxis response.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ot/1ot9_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ot/1ot9_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>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=1ot9 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Eight high-resolution crystal structures of the ground state of photoactive yellow protein (PYP) solved under a variety of conditions reveal that its chromophore is stabilized by two unusually short hydrogen bonds. Both Tyr42 Oeta and Glu46 Oepsilon are separated from the chromophore phenolate oxygen by less than the sum of their atomic van der Waals radii, 2.6 angstroms. This is characteristic of strong hydrogen bonding, in which hydrogen bonds acquire significant covalent character. The hydrogen bond from the protonated Glu46 to the negatively charged phenolate oxygen is 2.58 +/- 0.01 angstroms in length, while that from Tyr42 is considerably shorter, 2.49 +/- 0.01 angstroms. The E46Q mutant was solved to 0.95 angstroms resolution; the isosteric mutation increased the length of the hydrogen bond from Glx46 to the chromophore by 0.29 +/- 0.01 angstroms to that of an average hydrogen bond, 2.88 +/- 0.01 angstroms. The very short hydrogen bond from Tyr42 explains why mutating this residue has such a severe effect on the ground-state structure and PYP photocycle. The effect of isosteric mutations on the photocycle can be largely explained by the alterations to the length and strength of these hydrogen bonds.
Short hydrogen bonds in photoactive yellow protein.,Anderson S, Crosson S, Moffat K Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1008-16. Epub 2004, May 21. PMID:15159559<ref>PMID:15159559</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ot9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dsm 244]]
[[Category: Halorhodospira halophila]]
[[Category: Anderson, S]]
[[Category: Large Structures]]
[[Category: Crosson, S]]
[[Category: Anderson S]]
[[Category: Moffat, K]]
[[Category: Crosson S]]
[[Category: Cryotrapping]]
[[Category: Moffat K]]
[[Category: Luminescent protein]]
[[Category: Pyp]]

Latest revision as of 08:50, 17 April 2024

CRYOTRAPPED STATE IN WILD TYPE PHOTOACTIVE YELLOW PROTEIN, INDUCED WITH CONTINUOUS ILLUMINATION AT 110KCRYOTRAPPED STATE IN WILD TYPE PHOTOACTIVE YELLOW PROTEIN, INDUCED WITH CONTINUOUS ILLUMINATION AT 110K

Structural highlights

1ot9 is a 1 chain structure with sequence from Halorhodospira halophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

1ot9, resolution 1.00Å

Drag the structure with the mouse to rotate

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OCA
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