6ovh: Difference between revisions
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<StructureSection load='6ovh' size='340' side='right'caption='[[6ovh]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='6ovh' size='340' side='right'caption='[[6ovh]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ovh]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OVH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OVH FirstGlance]. <br> | <table><tr><td colspan='2'>[[6ovh]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OVH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OVH FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HAE:ACETOHYDROXAMIC+ACID'>HAE</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HAE:ACETOHYDROXAMIC+ACID'>HAE</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cybC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=6ovh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ovh OCA], [http://pdbe.org/6ovh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ovh RCSB], [http://www.ebi.ac.uk/pdbsum/6ovh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ovh ProSAT]</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=6ovh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ovh OCA], [http://pdbe.org/6ovh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ovh RCSB], [http://www.ebi.ac.uk/pdbsum/6ovh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ovh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX]] Electron-transport protein of unknown function. | [[http://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX]] Electron-transport protein of unknown function. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Many proteins exist naturally as symmetrical homooligomers or homopolymers(1). The emergent structural and functional properties of such protein assemblies have inspired extensive efforts in biomolecular design(2-5). As synthesized by ribosomes, proteins are inherently asymmetric. Thus, they must acquire multiple surface patches that selectively associate to generate the different symmetry elements needed to form higher-order architectures(1,6)-a daunting task for protein design. Here we address this problem using an inorganic chemical approach, whereby multiple modes of protein-protein interactions and symmetry are simultaneously achieved by selective, 'one-pot' coordination of soft and hard metal ions. We show that a monomeric protein (protomer) appropriately modified with biologically inspired hydroxamate groups and zinc-binding motifs assembles through concurrent Fe(3+) and Zn(2+) coordination into discrete dodecameric and hexameric cages. Our cages closely resemble natural polyhedral protein architectures(7,8) and are, to our knowledge, unique among designed systems(9-13) in that they possess tightly packed shells devoid of large apertures. At the same time, they can assemble and disassemble in response to diverse stimuli, owing to their heterobimetallic construction on minimal interprotein-bonding footprints. With stoichiometries ranging from [2 Fe:9 Zn:6 protomers] to [8 Fe:21 Zn:12 protomers], these protein cages represent some of the compositionally most complex protein assemblies-or inorganic coordination complexes-obtained by design. | |||
Constructing protein polyhedra via orthogonal chemical interactions.,Golub E, Subramanian RH, Esselborn J, Alberstein RG, Bailey JB, Chiong JA, Yan X, Booth T, Baker TS, Tezcan FA Nature. 2020 Jan 22. pii: 10.1038/s41586-019-1928-2. doi:, 10.1038/s41586-019-1928-2. PMID:31969701<ref>PMID:31969701</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ovh" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus coli migula 1895]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Alberstein, R G]] | [[Category: Alberstein, R G]] | ||
Revision as of 12:02, 5 February 2020
Cryo-EM structure of Bimetallic dodecameric cage design 3 (BMC3) from cytochrome cb562Cryo-EM structure of Bimetallic dodecameric cage design 3 (BMC3) from cytochrome cb562
Structural highlights
Function[C562_ECOLX] Electron-transport protein of unknown function. Publication Abstract from PubMedMany proteins exist naturally as symmetrical homooligomers or homopolymers(1). The emergent structural and functional properties of such protein assemblies have inspired extensive efforts in biomolecular design(2-5). As synthesized by ribosomes, proteins are inherently asymmetric. Thus, they must acquire multiple surface patches that selectively associate to generate the different symmetry elements needed to form higher-order architectures(1,6)-a daunting task for protein design. Here we address this problem using an inorganic chemical approach, whereby multiple modes of protein-protein interactions and symmetry are simultaneously achieved by selective, 'one-pot' coordination of soft and hard metal ions. We show that a monomeric protein (protomer) appropriately modified with biologically inspired hydroxamate groups and zinc-binding motifs assembles through concurrent Fe(3+) and Zn(2+) coordination into discrete dodecameric and hexameric cages. Our cages closely resemble natural polyhedral protein architectures(7,8) and are, to our knowledge, unique among designed systems(9-13) in that they possess tightly packed shells devoid of large apertures. At the same time, they can assemble and disassemble in response to diverse stimuli, owing to their heterobimetallic construction on minimal interprotein-bonding footprints. With stoichiometries ranging from [2 Fe:9 Zn:6 protomers] to [8 Fe:21 Zn:12 protomers], these protein cages represent some of the compositionally most complex protein assemblies-or inorganic coordination complexes-obtained by design. Constructing protein polyhedra via orthogonal chemical interactions.,Golub E, Subramanian RH, Esselborn J, Alberstein RG, Bailey JB, Chiong JA, Yan X, Booth T, Baker TS, Tezcan FA Nature. 2020 Jan 22. pii: 10.1038/s41586-019-1928-2. doi:, 10.1038/s41586-019-1928-2. PMID:31969701[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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