6vp3: Difference between revisions
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==Artificial Metalloproteins with Dinuclear Iron Centers== | ==Artificial Metalloproteins with Dinuclear Iron Centers== | ||
<StructureSection load='6vp3' size='340' side='right'caption='[[6vp3]]' scene=''> | <StructureSection load='6vp3' size='340' side='right'caption='[[6vp3]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VP3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6vp3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VP3 FirstGlance]. <br> | ||
</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=6vp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vp3 OCA], [https://pdbe.org/6vp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vp3 RCSB], [https://www.ebi.ac.uk/pdbsum/6vp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vp3 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=KM3:{N-(4-{bis[(pyridin-2-yl-kappaN)methyl]amino-kappaN}butyl)-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide}iron(3+)'>KM3</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=6vp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vp3 OCA], [https://pdbe.org/6vp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vp3 RCSB], [https://www.ebi.ac.uk/pdbsum/6vp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vp3 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Dinuclear iron centers with a bridging hydroxido or oxido ligand form active sites within a variety of metalloproteins. A key feature of these sites is the ability of the protein to control the structures around the Fe centers, which leads to entatic states that are essential for function. To simulate this controlled environment, artificial proteins have been engineered using biotin-streptavidin (Sav) technology in which Fe complexes from adjacent subunits can assemble to form [Fe(III)-(mu-OH)-Fe(III)] cores. The assembly process is promoted by the site-specific localization of the Fe complexes within a subunit through the designed mutation of a tyrosinate side chain to coordinate the Fe centers. An important outcome is that the Sav host can regulate the Fe...Fe separation, which is known to be important for function in natural metalloproteins. Spectroscopic and structural studies from X-ray diffraction methods revealed uncommonly long Fe...Fe separations that change by less than 0.3 A upon the binding of additional bridging ligands. The structural constraints imposed by the protein host on the di-Fe cores are unique and create examples of active sites having entatic states within engineered artificial metalloproteins. | |||
Artificial Metalloproteins with Dinuclear Iron-Hydroxido Centers.,Miller KR, Biswas S, Jasniewski A, Follmer AH, Biswas A, Albert T, Sabuncu S, Bominaar EL, Hendrich MP, Moenne-Loccoz P, Borovik AS J Am Chem Soc. 2021 Feb 10;143(5):2384-2393. doi: 10.1021/jacs.0c12564. Epub 2021 , Feb 2. PMID:33528256<ref>PMID:33528256</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6vp3" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Avidin 3D structures|Avidin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Streptomyces avidinii]] | |||
[[Category: Albert T]] | [[Category: Albert T]] | ||
[[Category: Biswas S]] | [[Category: Biswas S]] | ||
Latest revision as of 11:16, 11 October 2023
Artificial Metalloproteins with Dinuclear Iron CentersArtificial Metalloproteins with Dinuclear Iron Centers
Structural highlights
FunctionSAV_STRAV The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). Publication Abstract from PubMedDinuclear iron centers with a bridging hydroxido or oxido ligand form active sites within a variety of metalloproteins. A key feature of these sites is the ability of the protein to control the structures around the Fe centers, which leads to entatic states that are essential for function. To simulate this controlled environment, artificial proteins have been engineered using biotin-streptavidin (Sav) technology in which Fe complexes from adjacent subunits can assemble to form [Fe(III)-(mu-OH)-Fe(III)] cores. The assembly process is promoted by the site-specific localization of the Fe complexes within a subunit through the designed mutation of a tyrosinate side chain to coordinate the Fe centers. An important outcome is that the Sav host can regulate the Fe...Fe separation, which is known to be important for function in natural metalloproteins. Spectroscopic and structural studies from X-ray diffraction methods revealed uncommonly long Fe...Fe separations that change by less than 0.3 A upon the binding of additional bridging ligands. The structural constraints imposed by the protein host on the di-Fe cores are unique and create examples of active sites having entatic states within engineered artificial metalloproteins. Artificial Metalloproteins with Dinuclear Iron-Hydroxido Centers.,Miller KR, Biswas S, Jasniewski A, Follmer AH, Biswas A, Albert T, Sabuncu S, Bominaar EL, Hendrich MP, Moenne-Loccoz P, Borovik AS J Am Chem Soc. 2021 Feb 10;143(5):2384-2393. doi: 10.1021/jacs.0c12564. Epub 2021 , Feb 2. PMID:33528256[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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