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1yk4
From Proteopedia
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| - | [[Image:1yk4.gif|left|200px]]<br /><applet load="1yk4" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1yk4, resolution 0.69Å" /> | ||
| - | '''Ultra-high resolution structure of Pyrococcus abyssi rubredoxin W4L/R5S'''<br /> | ||
| - | == | + | ==Ultra-high resolution structure of Pyrococcus abyssi rubredoxin W4L/R5S== |
| + | <StructureSection load='1yk4' size='340' side='right'caption='[[1yk4]], [[Resolution|resolution]] 0.69Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1yk4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YK4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.69Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</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=1yk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yk4 OCA], [https://pdbe.org/1yk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yk4 RCSB], [https://www.ebi.ac.uk/pdbsum/1yk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yk4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RUBR_PYRAB RUBR_PYRAB] 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 (By similarity). | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yk/1yk4_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </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/main_output.php?pdb_ID=1yk4 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The crystal structure of Pyrococcus abyssi rubredoxin mutant W4L/R5S was solved by direct methods. The model of the air-oxidized protein was refined by partially restrained full-matrix least-squares refinement against intensity data to 0.69 A resolution. This first ultrahigh-resolution structure of a rubredoxin provides very detailed and precise information about the Fe(SCys)(4) centre and its environment, the peptide-backbone stereochemistry, H atoms and hydrogen bonds, static and dynamic disorder, the solvent structure and the electron-density distribution. P. abyssi rubredoxin W4L/R5S is the first of a series of mutants studied by atomic and ultrahigh-resolution X-ray crystallography which are expected to contribute to the understanding of structure-function relationships in iron-sulfur proteins. | The crystal structure of Pyrococcus abyssi rubredoxin mutant W4L/R5S was solved by direct methods. The model of the air-oxidized protein was refined by partially restrained full-matrix least-squares refinement against intensity data to 0.69 A resolution. This first ultrahigh-resolution structure of a rubredoxin provides very detailed and precise information about the Fe(SCys)(4) centre and its environment, the peptide-backbone stereochemistry, H atoms and hydrogen bonds, static and dynamic disorder, the solvent structure and the electron-density distribution. P. abyssi rubredoxin W4L/R5S is the first of a series of mutants studied by atomic and ultrahigh-resolution X-ray crystallography which are expected to contribute to the understanding of structure-function relationships in iron-sulfur proteins. | ||
| - | + | Ultrahigh-resolution study on Pyrococcus abyssi rubredoxin. I. 0.69 A X-ray structure of mutant W4L/R5S.,Bonisch H, Schmidt CL, Bianco P, Ladenstein R Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):990-1004. Epub 2005, Jun 24. PMID:15983423<ref>PMID:15983423</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1yk4" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Hydrogen in macromolecular models|Hydrogen in macromolecular models]] | ||
| + | *[[Rubredoxin 3D structures|Rubredoxin 3D structures]] | ||
| + | *[[Rubredoxin PDB structures|Rubredoxin PDB structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pyrococcus abyssi]] | ||
| + | [[Category: Bianco P]] | ||
| + | [[Category: Bonisch H]] | ||
| + | [[Category: Ladenstein R]] | ||
| + | [[Category: Schmidt CL]] | ||
Current revision
Ultra-high resolution structure of Pyrococcus abyssi rubredoxin W4L/R5S
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