1m9w
From Proteopedia
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==Study of electrostatic potential surface distribution using high resolution side-chain conformation determined by NMR== | ==Study of electrostatic potential surface distribution using high resolution side-chain conformation determined by NMR== | ||
| - | <StructureSection load='1m9w' size='340' side='right'caption='[[1m9w | + | <StructureSection load='1m9w' size='340' side='right'caption='[[1m9w]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1m9w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M9W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M9W FirstGlance]. <br> | <table><tr><td colspan='2'>[[1m9w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M9W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M9W FirstGlance]. <br> | ||
| - | </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=1m9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m9w OCA], [https://pdbe.org/1m9w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m9w RCSB], [https://www.ebi.ac.uk/pdbsum/1m9w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m9w ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1m9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m9w OCA], [https://pdbe.org/1m9w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m9w RCSB], [https://www.ebi.ac.uk/pdbsum/1m9w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m9w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/PLAS_SYNY3 PLAS_SYNY3] Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.[HAMAP-Rule:MF_00566] | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1m9w 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=1m9w ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Plastocyanin is a small (approximately 10 kDa), type I blue copper protein that works as an electron donor to photosystem I from cytochrome f in both chloroplast systems and in some strains of cyanobacteria. Comparative studies of the kinetic mechanisms of plastocyanins in different organisms show that the electron transfer from photosystem I happens by simple collision in cyanobacteria but through a intermediate transition complex in green algae and superior plants. Previous work has proved that this effect cannot be explained by structural variations across the different plastocyanins but it can be explained by differences in the electrostatic potential distribution at the protein surface. In that case, minor conformational errors at the amino acid side chain level may imply an important effect in the electrostatic potential distribution calculation. In this work we present a high resolution study of side chain conformation by homonuclear NMR for the reduced wild-type plastocyanin Synechocystis using intensity ratios for 2D-NOESY and 2D-H,H-TOCSY cross peaks at different mixing times. We also present the corresponding comparison with different plastocyanin structures and the effect in the electrostatic potential distribution at the protein surface. We discuss the importance of indirect J-coupling information from TOCSY-type experiments as complement for intraresidue distances derived from NOESY experiments in the determination of side chain orientation and stereo-specific assignments. | ||
| - | + | ==See Also== | |
| - | + | *[[Plastocyanin 3D structures|Plastocyanin 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Synechocystis sp]] | [[Category: Synechocystis sp]] | ||
| - | [[Category: Celda | + | [[Category: Celda B]] |
| - | [[Category: Monleon | + | [[Category: Monleon D]] |
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Revision as of 08:33, 10 April 2024
Study of electrostatic potential surface distribution using high resolution side-chain conformation determined by NMR
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