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TitleConstructing protein polyhedra via orthogonal chemical interactions.
Journal, issue, pagesNature, Vol. 578, Issue 7793, Page 172-176, Year 2020
Publish dateJan 22, 2020
AuthorsEyal Golub / Rohit H Subramanian / Julian Esselborn / Robert G Alberstein / Jake B Bailey / Jerika A Chiong / Xiaodong Yan / Timothy Booth / Timothy S Baker / F Akif Tezcan /
PubMed AbstractMany proteins exist naturally as symmetrical homooligomers or homopolymers. The emergent structural and functional properties of such protein assemblies have inspired extensive efforts in ...Many proteins exist naturally as symmetrical homooligomers or homopolymers. The emergent structural and functional properties of such protein assemblies have inspired extensive efforts in biomolecular design. 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-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 and Zn coordination into discrete dodecameric and hexameric cages. Our cages closely resemble natural polyhedral protein architectures and are, to our knowledge, unique among designed systems 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.
External linksNature / PubMed:31969701 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.4 - 2.6 Å
Structure data

20212

6ovh

EMDB-20212, PDB-6ovh:
Cryo-EM structure of Bimetallic dodecameric cage design 3 (BMC3) from cytochrome cb562
Method: EM (single particle) / Resolution: 2.6 Å

PDB-6ot4:
Bimetallic dodecameric cage design 2 (BMC2) from cytochrome cb562
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-6ot7:
Bimetallic dodecameric cage design 3 (BMC3) from cytochrome cb562
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-6ot8:
Bimetallic hexameric cage design 4 (BMC4) from cytochrome cb562
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-6ot9:
Bimetallic dodecameric cage design 1 (BMC1) from cytochrome cb562
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-HEC:
HEME C / Heme C

ChemComp-HAE:
ACETOHYDROXAMIC ACID / inhibitor, medication*YM / Acetohydroxamic acid

ChemComp-FE:
Unknown entry / Iron

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER / Water

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM / Polyethylene glycol

Source
  • escherichia coli (E. coli)
KeywordsMETAL BINDING PROTEIN / Supramolecular assembly / protein cage / bimetallic / metal binding / hydroxamic acid

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