1adw: Difference between revisions
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==PSEUDOAZURIN== | ==PSEUDOAZURIN== | ||
<StructureSection load='1adw' size='340' side='right' caption='[[1adw]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1adw' size='340' side='right' caption='[[1adw]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
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<table><tr><td colspan='2'>[[1adw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Paracoccus_pantotrophus Paracoccus pantotrophus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ADW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ADW FirstGlance]. <br> | <table><tr><td colspan='2'>[[1adw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Paracoccus_pantotrophus Paracoccus pantotrophus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ADW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ADW FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=1adw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1adw OCA], [http://pdbe.org/1adw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1adw RCSB], [http://www.ebi.ac.uk/pdbsum/1adw PDBsum]</span></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=1adw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1adw OCA], [http://pdbe.org/1adw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1adw RCSB], [http://www.ebi.ac.uk/pdbsum/1adw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1adw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1adw ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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[[Category: Paracoccus pantotrophus]] | [[Category: Paracoccus pantotrophus]] | ||
[[Category: Williams, P A]] | [[Category: Williams, P A]] | ||
[[Category: Copper]] | |||
[[Category: Cuproprotein]] | [[Category: Cuproprotein]] | ||
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
Revision as of 12:13, 9 August 2017
PSEUDOAZURINPSEUDOAZURIN
Structural highlights
Function[AZUP_PARPN] This soluble electron transfer copper protein is required for the inactivation of copper-containing nitrite reductase in the presence of oxygen. 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 PubMedThe structure of pseudoazurin from Thiosphaera pantotropha has been determined and compared to structures of both soluble and membrane-bound periplasmic redox proteins. The results show a matching set of unipolar, but promiscuous, docking motifs based on a positive hydrophobic surface patch on the electron shuttle proteins pseudoazurin and cytochrome c550 and a negative hydrophobic patch on the surface of their known redox partners. The observed electrostatic handedness is argued to be associated with the charge-asymmetry of the membrane-bound components of the redox chain due to von Heijne's 'positives-inside' principle. We propose a 'positives-in-between' rule for electron shuttle proteins, and expect a negative hydrophobic patch to be present on both the highest and lowest redox potential species in a series of electron carriers. Pseudospecific docking surfaces on electron transfer proteins as illustrated by pseudoazurin, cytochrome c550 and cytochrome cd1 nitrite reductase.,Williams PA, Fulop V, Leung YC, Chan C, Moir JW, Howlett G, Ferguson SJ, Radford SE, Hajdu J Nat Struct Biol. 1995 Nov;2(11):975-82. PMID:7583671[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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