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| | <StructureSection load='2vu4' size='340' side='right'caption='[[2vu4]], [[Resolution|resolution]] 1.98Å' scene=''> | | <StructureSection load='2vu4' size='340' side='right'caption='[[2vu4]], [[Resolution|resolution]] 1.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vu4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Spiol Spiol]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VU4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vu4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VU4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.98Å</td></tr> |
| | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2vu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vu4 OCA], [https://pdbe.org/2vu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vu4 RCSB], [https://www.ebi.ac.uk/pdbsum/2vu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vu4 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=2vu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vu4 OCA], [https://pdbe.org/2vu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vu4 RCSB], [https://www.ebi.ac.uk/pdbsum/2vu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vu4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PSBP_SPIOL PSBP_SPIOL]] May be involved in the regulation of photosystem II.
| + | [https://www.uniprot.org/uniprot/PSBP_SPIOL PSBP_SPIOL] May be involved in the regulation of photosystem II. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Photosystem II|Photosystem II]] | + | *[[Photosystem II 3D structures|Photosystem II 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Spiol]] | + | [[Category: Spinacia oleracea]] |
| - | [[Category: Arellano, J B]] | + | [[Category: Arellano JB]] |
| - | [[Category: Ettrich, R]] | + | [[Category: Ettrich R]] |
| - | [[Category: Lapkouski, M]]
| + | [[Category: Kuta Smatanova I]] |
| - | [[Category: Revuelta, J L]]
| + | [[Category: Lapkouski M]] |
| - | [[Category: Ristvejova, R]]
| + | [[Category: Revuelta JL]] |
| - | [[Category: Smatanova, I Kuta]] | + | [[Category: Ristvejova R]] |
| - | [[Category: 23 kda protein]] | + | |
| - | [[Category: Chloroplast]] | + | |
| - | [[Category: Higher plant]] | + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Oxygen-evolving complex]]
| + | |
| - | [[Category: Photosynthesis]]
| + | |
| - | [[Category: Photosystem ii]]
| + | |
| - | [[Category: Thylakoid]]
| + | |
| - | [[Category: Transit peptide]]
| + | |
| Structural highlights
Function
PSBP_SPIOL May be involved in the regulation of photosystem II.
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
Raman microscopy permits structural analysis of protein crystals in situ in hanging drops, allowing for comparison with Raman measurements in solution. Nevertheless, the two methods sometimes reveal subtle differences in structure that are often ascribed to the water layer surrounding the protein. The novel method of drop-coating deposition Raman spectropscopy (DCDR) exploits an intermediate phase that, although nominally "dry," has been shown to preserve protein structural features present in solution. The potential of this new approach to bridge the structural gap between proteins in solution and in crystals is explored here with extrinsic protein PsbP of photosystem II from Spinacia oleracea. In the high-resolution (1.98 A) x-ray crystal structure of PsbP reported here, several segments of the protein chain are present but unresolved. Analysis of the three kinds of Raman spectra of PsbP suggests that most of the subtle differences can indeed be attributed to the water envelope, which is shown here to have a similar Raman intensity in glassy and crystal states. Using molecular dynamics simulations cross-validated by Raman solution data, two unresolved segments of the PsbP crystal structure were modeled as loops, and the amino terminus was inferred to contain an additional beta segment. The complete PsbP structure was compared with that of the PsbP-like protein CyanoP, which plays a more peripheral role in photosystem II function. The comparison suggests possible interaction surfaces of PsbP with higher-plant photosystem II. This work provides the first complete structural picture of this key protein, and it represents the first systematic comparison of Raman data from solution, glassy, and crystalline states of a protein.
Raman Spectroscopy Adds Complementary Detail to the High-Resolution X-Ray Crystal Structure of Photosynthetic PsbP from Spinacia oleracea.,Kopecky V Jr, Kohoutova J, Lapkouski M, Hofbauerova K, Sovova Z, Ettrichova O, Gonzalez-Perez S, Dulebo A, Kaftan D, Kuta Smatanova I, Revuelta JL, Arellano JB, Carey J, Ettrich R PLoS One. 2012;7(10):e46694. doi: 10.1371/journal.pone.0046694. Epub 2012 Oct 5. PMID:23071614[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kopecky V Jr, Kohoutova J, Lapkouski M, Hofbauerova K, Sovova Z, Ettrichova O, Gonzalez-Perez S, Dulebo A, Kaftan D, Kuta Smatanova I, Revuelta JL, Arellano JB, Carey J, Ettrich R. Raman Spectroscopy Adds Complementary Detail to the High-Resolution X-Ray Crystal Structure of Photosynthetic PsbP from Spinacia oleracea. PLoS One. 2012;7(10):e46694. doi: 10.1371/journal.pone.0046694. Epub 2012 Oct 5. PMID:23071614 doi:http://dx.doi.org/10.1371/journal.pone.0046694
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