PDBsum entry 6ovh

Metal binding protein

PDB id: 6ovh

Contents

Protein chains

(+ 6 more) 106 a.a.

Ligands

HEC ×12

HAE ×24

Metals

_FE ×8

_ZN ×24

Waters ×171

PDB id:

6ovh

Name:

Metal binding protein

Title:

Cryo-em structure of bimetallic dodecameric cage design 3 (bmc3) from cytochrome cb562

Structure:

Soluble cytochrome b562. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Synonym: cytochrome b-562. Engineered: yes. Mutation: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: cybc. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: bl21(de3).

Authors:

E.Golub,R.H.Subramanian,X.Yan,R.G.Alberstein,F.A.Tezcan

Key ref:

E.Golub et al. (2020). Constructing protein polyhedra via orthogonal chemical interactions. Nature, 578, 172-176. PubMed id: 31969701 DOI: 10.1038/s41586-019-1928-2

Date:

07-May-19 Release date: 29-Jan-20

Protein chains

P0ABE7  (C562_ECOLX) -  Soluble cytochrome b562 from Escherichia coli

Seq: 128 a.a.

Struc: 106 a.a.*

* PDB and UniProt seqs differ at 22 residue positions (black crosses)

DOI no: 10.1038/s41586-019-1928-2

Nature 578:172-176 (2020)

PubMed id: 31969701

Constructing protein polyhedra via orthogonal chemical interactions.

E.Golub, R.H.Subramanian, J.Esselborn, R.G.Alberstein, J.B.Bailey, J.A.Chiong, X.Yan, T.Booth, T.S.Baker, F.A.Tezcan.

ABSTRACT

Many proteins exist naturally as symmetrical homooligomers or homopolymers¹. 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 Fe³⁺ and Zn²⁺ 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.