5ai3: Difference between revisions
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<StructureSection load='5ai3' size='340' side='right'caption='[[5ai3]], [[Resolution|resolution]] 1.02Å' scene=''> | <StructureSection load='5ai3' size='340' side='right'caption='[[5ai3]], [[Resolution|resolution]] 1.02Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ai3]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ai3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AI3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</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=5ai3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ai3 OCA], [https://pdbe.org/5ai3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ai3 RCSB], [https://www.ebi.ac.uk/pdbsum/5ai3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ai3 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/RUBR_PYRFU RUBR_PYRFU] Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5ai3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ai3" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Rubredoxin 3D structures|Rubredoxin 3D structures]] | |||
*[[Rubredoxin PDB structures|Rubredoxin PDB structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
[[Category: Cuypers | [[Category: Cuypers MG]] | ||
[[Category: Mitchell | [[Category: Mitchell EP]] | ||
Revision as of 08:00, 25 May 2023
X-ray structure of 113Cd-substituted Perdeuterated Pyrococcus furiosus rubredoxin to 1.02A resolution at 295K in a quartz capillaryX-ray structure of 113Cd-substituted Perdeuterated Pyrococcus furiosus rubredoxin to 1.02A resolution at 295K in a quartz capillary
Structural highlights
FunctionRUBR_PYRFU Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. Publication Abstract from PubMedIn this report we show for the first time that neutron anomalous dispersion can be used in a practical manner to determine experimental phases of a protein crystal structure, providing a new tool for structural biologists. The approach is demonstrated through the use of a state-of-the-art monochromatic neutron diffractometer at the Institut Laue-Langevin (ILL) in combination with crystals of perdeuterated protein that minimise the level of hydrogen incoherent scattering and enhance the visibility of the anomalous signal. The protein used was rubredoxin in which cadmium replaced the iron at the iron-sulphur site. While this study was carried out using a steady-state neutron beam source, the results will be of major interest for capabilities at existing and emerging spallation neutron sources where time-of-flight instruments provide inherent energy discrimination. In particular this capability may be expected to offer unique opportunities to a rapidly developing structural biology community where there is increasing interest in the identification of protonation states, protein/water interactions and protein-ligand interactions - all of which are of central importance to a wide range of fundamental and applied areas in the biosciences. Macromolecular structure phasing by neutron anomalous diffraction.,Cuypers MG, Mason SA, Mossou E, Haertlein M, Forsyth VT, Mitchell EP Sci Rep. 2016 Aug 11;6:31487. doi: 10.1038/srep31487. PMID:27511806[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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