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| | <StructureSection load='1gsw' size='340' side='right'caption='[[1gsw]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='1gsw' size='340' side='right'caption='[[1gsw]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gsw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GSW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gsw]] 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=1GSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GSW 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]] 1.85Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d7e|1d7e]], [[1gsv|1gsv]], [[1gsx|1gsx]], [[1f98|1f98]], [[1f9i|1f9i]], [[2phy|2phy]], [[2pyp|2pyp]], [[2pyr|2pyr]], [[3phy|3phy]], [[3pyp|3pyp]]</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='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=1gsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gsw OCA], [http://pdbe.org/1gsw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gsw RCSB], [http://www.ebi.ac.uk/pdbsum/1gsw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gsw ProSAT]</span></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=1gsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gsw OCA], [https://pdbe.org/1gsw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gsw RCSB], [https://www.ebi.ac.uk/pdbsum/1gsw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gsw ProSAT]</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]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Halorhodospira halophila]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aalten, D M.F Van]]
| + | [[Category: Crielaard W]] |
| - | [[Category: Crielaard, W]] | + | [[Category: Hellingwerf KJ]] |
| - | [[Category: Hellingwerf, K J]] | + | [[Category: Joshua-Tor L]] |
| - | [[Category: Joshua-Tor, L]] | + | [[Category: Van Aalten DMF]] |
| - | [[Category: Photoreceptor]] | + | |
| - | [[Category: Photosynthesis]]
| + | |
| 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 PubMed
Crystallographic and spectroscopic analyses of three hinge-bending mutants of the photoactive yellow protein are described. Previous studies have identified Gly(47) and Gly(51) as possible hinge points in the structure of the protein, allowing backbone segments around the chromophore to undergo large concerted motions. We have designed, crystallized, and solved the structures of three mutants: G47S, G51S, and G47S/G51S. The protein dynamics of these mutants are significantly affected. Transitions in the photocycle, measured with laser induced transient absorption spectroscopy, show rates up to 6-fold different from the wild type protein and show an additive effect in the double mutant. Compared with the native structure, no significant conformational differences were observed in the structures of the mutant proteins. We conclude that the structural and dynamic integrity of the region around these mutations is of crucial importance to the photocycle and suggest that the hinge-bending properties of Gly(51) may also play a role in PAS domain proteins where it is one of the few conserved residues.
Engineering photocycle dynamics. Crystal structures and kinetics of three photoactive yellow protein hinge-bending mutants.,van Aalten DM, Haker A, Hendriks J, Hellingwerf KJ, Joshua-Tor L, Crielaard W J Biol Chem. 2002 Feb 22;277(8):6463-8. Epub 2001 Nov 19. PMID:11714713[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van Aalten DM, Haker A, Hendriks J, Hellingwerf KJ, Joshua-Tor L, Crielaard W. Engineering photocycle dynamics. Crystal structures and kinetics of three photoactive yellow protein hinge-bending mutants. J Biol Chem. 2002 Feb 22;277(8):6463-8. Epub 2001 Nov 19. PMID:11714713 doi:10.1074/jbc.M109313200
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