PDBsum entry 6ruh

Protein binding

PDB id: 6ruh

Contents

Protein chain

279 a.a.

Ligands

WNI ×2

SO4

Waters ×349

PDB id:

6ruh

Name:

Protein binding

Title:

Ni-substituted alpha-keggin bound to proteinase k solved by mr

Structure:

Proteinase k. Chain: a. Synonym: endopeptidase k,tritirachium alkaline proteinase. Ec: 3.4.21.64

Source:

Parengyodontium album. Tritirachium album. Organism_taxid: 37998

Resolution:

1.10Å R-factor: 0.147 R-free: 0.158

Authors:

J.Breibeck,A.Bijelic,A.Rompel

Key ref:

J.Breibeck et al. (2019). Transition metal-substituted Keggin polyoxotungstates enabling covalent attachment to proteinase K upon co-crystallization. Chem Commun (Camb), 55, 11519-11522. PubMed id: 31490500 DOI: 10.1039/c9cc05818d

Date:

28-May-19 Release date: 18-Sep-19

Protein chain

P06873  (PRTK_PARAQ) -  Proteinase K from Parengyodontium album

Seq: 384 a.a.

Struc: 279 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.4.21.64 - peptidase K.
• Reaction: Hydrolysis of keratin and of other proteins, with subtilisin-like specificity. Hydrolyzes peptides amides.

DOI no: 10.1039/c9cc05818d

Chem Commun (Camb) 55:11519-11522 (2019)

PubMed id: 31490500

Transition metal-substituted Keggin polyoxotungstates enabling covalent attachment to proteinase K upon co-crystallization.

J.Breibeck, A.Bijelic, A.Rompel.

ABSTRACT

The use of α- and β-Keggin polyoxotungstates (POTs) substituted by a single first row transition metal ion (CoII, NiII, CuII, ZnII) as superchaotropic crystallization additives led to covalent and non-covalent interactions with protein side-chains of proteinase K. Two major Keggin POT binding sites in proteinase K were identified, both stabilizing the orientation of the substituted metal site towards the protein surface and suggesting increased protein affinity for the substitution sites. The formation of all observed covalent bonds involves the same aspartate carboxylate, taking the role of a terminal oxygen with the Keggin α-isomer or even, in an unprecedented scenario, a bridging cluster oxygen with the β-isomer. Covalent bond formation with the protein carboxylate was observed only with the NiII- and CoII-substituted POTs, following the HSAB concept and the principle of metal immobilization.