1h7v
From Proteopedia
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==Rubredoxin from Guillardia Theta== | ==Rubredoxin from Guillardia Theta== | ||
- | <StructureSection load='1h7v' size='340' side='right'caption='[[1h7v | + | <StructureSection load='1h7v' size='340' side='right'caption='[[1h7v]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1h7v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1h7v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Guillardia_theta Guillardia theta]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H7V FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </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=' | + | <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=1h7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h7v OCA], [https://pdbe.org/1h7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h7v RCSB], [https://www.ebi.ac.uk/pdbsum/1h7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h7v 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=1h7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h7v OCA], [https://pdbe.org/1h7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h7v RCSB], [https://www.ebi.ac.uk/pdbsum/1h7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h7v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q9XG40_GUITH Q9XG40_GUITH] | ||
== 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=1h7v 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=1h7v ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The rubredoxin from the cryptomonad Guillardia theta is one of the first examples of a rubredoxin encoded in a eukaryotic organism. The structure of a soluble zinc-substituted 70-residue G. theta rubredoxin lacking the membrane anchor and the thylakoid targeting sequence was determined by multidimensional heteronuclear NMR, representing the first three-dimensional (3D) structure of a eukaryotic rubredoxin. For the structure calculation a strategy was applied in which information about hydrogen bonds was directly inferred from a long-range HNCO experiment, and the dynamics of the protein was deduced from heteronuclear nuclear Overhauser effect data and exchange rates of the amide protons. The structure is well defined, exhibiting average root-mean-square deviations of 0.21 A for the backbone heavy atoms and 0.67 A for all heavy atoms of residues 7-56, and an increased flexibility toward the termini. The structure of this core fold is almost identical to that of prokaryotic rubredoxins. There are, however, significant differences with respect to the charge distribution at the protein surface, suggesting that G. theta rubredoxin exerts a different physiological function compared to the structurally characterized prokaryotic rubredoxins. The amino-terminal residues containing the putative signal peptidase recognition/cleavage site show an increased flexibility compared to the core fold, but still adopt a defined 3D orientation, which is mainly stabilized by nonlocal interactions to residues of the carboxy-terminal region. This orientation might reflect the structural elements and charge pattern necessary for correct signal peptidase recognition of the G. theta rubredoxin precursor. | ||
- | + | ==See Also== | |
- | + | *[[Rubredoxin 3D structures|Rubredoxin 3D structures]] | |
- | + | *[[Rubredoxin PDB structures|Rubredoxin PDB structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Guillardia theta]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Hoffmann | + | [[Category: Hoffmann S]] |
- | [[Category: Maier | + | [[Category: Maier UG]] |
- | [[Category: Roesch | + | [[Category: Roesch P]] |
- | [[Category: Schweimer | + | [[Category: Schweimer K]] |
- | [[Category: Sticht | + | [[Category: Sticht H]] |
- | [[Category: Wastl | + | [[Category: Wastl J]] |
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Revision as of 11:29, 27 March 2024
Rubredoxin from Guillardia Theta
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