5i26
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Azurin T30R1, crystal form I== | |
| + | <StructureSection load='5i26' size='340' side='right' caption='[[5i26]], [[Resolution|resolution]] 1.89Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5i26]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I26 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> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=R1A:3-{[(2,2,5,5-TETRAMETHYL-1-OXO-2,5-DIHYDRO-1H-PYRROLIUM-3-YL)METHYL]DISULFANYL}-D-ALANINE'>R1A</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=5i26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i26 OCA], [http://pdbe.org/5i26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i26 RCSB], [http://www.ebi.ac.uk/pdbsum/5i26 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE]] Transfers electrons from cytochrome c551 to cytochrome oxidase. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pulsed electron-electron double resonance (PELDOR or DEER) in combination with site-directed spin labelling has emerged as an important method for measuring nanometer distance constraints that are used to obtain coarse-grained structures of biomolecules or to follow their conformational changes. Translating measured spin-spin distances between spin labels into structural information requires taking the conformational flexibility of spin label side chains into account. Here, we present an analysis of orientation selective PELDOR data recorded on six singly MTSSL-labelled azurin mutants. The analysis yielded conformational MTSSL ensembles, which are considerably narrower than those predicted using in silico spin labeling methods but match well with spin label conformations found in the corresponding crystal structures. The possible reasons and consequences for predicting spin label conformers in the fold of biomolecules are discussed. | ||
| - | + | Determination of nitroxide spin label conformations via PELDOR and X-ray crystallography.,Abdullin D, Hagelueken G, Schiemann O Phys Chem Chem Phys. 2016 Apr 21;18(15):10428-37. doi: 10.1039/c6cp01307d. Epub, 2016 Mar 31. PMID:27029516<ref>PMID:27029516</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 5i26" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Hagelueken, G]] | [[Category: Hagelueken, G]] | ||
| + | [[Category: Blue copper protein]] | ||
| + | [[Category: Metal binding protein]] | ||
| + | [[Category: Spin label]] | ||
Revision as of 16:52, 10 May 2016
Azurin T30R1, crystal form I
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