PDBsum entry 6h8t

Metal binding protein

PDB id

6h8t

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Contents

			Protein chains

					214 a.a.

			Ligands

					ACT ×9


					YXZ


					YXX


					SO4

			Metals

					_CL


					_NA

			Waters ×332

PDB id:

6h8t

Links

Name:

Metal binding protein

Title:

Crystal structure of papain modify by achiral ru(ii)complex

Structure:

Papain. Chain: a, j. Synonym: papaya proteinase i,ppi. Engineered: yes. Other_details: cysteine 25 is covalently bound to a ruthenium complex. Tyr 61 and 67 are hydroxylated.

Source:

Carica papaya. Papaya. Organism_taxid: 3649. Expressed in: carica papaya. Expression_system_taxid: 3649

Resolution:

2.10Å

R-factor:

0.195

R-free:

0.249

Authors:

M.V.Cherrier,P.Amara,B.Talbi,M.Salmin,J.C.Fontecilla-Camps

Key ref:

M.V.Cherrier et al. (2018). Crystallographic evidence for unexpected selective tyrosine hydroxylations in an aerated achiral Ru-papain conjugate. Metallomics, 10, 1452-1459. PubMed id: 30175357 DOI: 10.1039/c8mt00160j

Date:

03-Aug-18

Release date:

12-Sep-18

Supersedes:

4kp9

PROCHECK

	Headers

	References

Protein chains

P00784 (PAPA1_CARPA) - Papain from Carica papaya

Seq: Struc:					345 a.a. 214 a.a.*

Key:

Secondary structure

* PDB and UniProt seqs differ at 2 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

E.C.3.4.22.2 - papain.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

Hydrolysis of proteins with broad specificity for peptide bonds, with preference for a residue bearing a large hydrophobic sidechain at the P2 position. Does not accept Val at P1'.

DOI no: 10.1039/c8mt00160j	Metallomics 10:1452-1459 (2018)
PubMed id: 30175357

Crystallographic evidence for unexpected selective tyrosine hydroxylations in an aerated achiral Ru-papain conjugate.
M.V.Cherrier, P.Amara, B.Talbi, M.Salmain, J.C.Fontecilla-Camps.

ABSTRACT

The X-ray structure of an aerated achiral Ru-papain conjugate has revealed the hydroxylation of two tyrosine residues found near the ruthenium ion. The most likely mechanism involves a ruthenium-bound superoxide as the reactive species responsible for the first hydroxylation and the resulting high valent Ru(iv)[double bond, length as m-dash]O species for the second one.