1ot9: Difference between revisions

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New page: left|200px<br /><applet load="1ot9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ot9, resolution 1.00Å" /> '''CRYOTRAPPED STATE IN...
 
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[[Image:1ot9.jpg|left|200px]]<br /><applet load="1ot9" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ot9, resolution 1.00&Aring;" />
'''CRYOTRAPPED STATE IN WILD TYPE PHOTOACTIVE YELLOW PROTEIN, INDUCED WITH CONTINUOUS ILLUMINATION AT 110K'''<br />


==Overview==
==CRYOTRAPPED STATE IN WILD TYPE PHOTOACTIVE YELLOW PROTEIN, INDUCED WITH CONTINUOUS ILLUMINATION AT 110K==
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.
<StructureSection load='1ot9' size='340' side='right'caption='[[1ot9]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
1OT9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halorhodospira_halophila Halorhodospira halophila] with HC4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OT9 OCA].
</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='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>
==Reference==
<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>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15159559 15159559]
</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/ot/1ot9_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=1ot9 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Halorhodospira halophila]]
[[Category: Halorhodospira halophila]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Anderson, S.]]
[[Category: Anderson S]]
[[Category: Crosson, S.]]
[[Category: Crosson S]]
[[Category: Moffat, K.]]
[[Category: Moffat K]]
[[Category: HC4]]
[[Category: cryotrapping]]
[[Category: pyp]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:10:40 2007''

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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