PDBsum entry 4z46

Hydrolase

PDB id

4z46

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Contents

			Protein chain

					129 a.a.

			Ligands

					EDO ×2


					NO3 ×9


					1PT


					CPT

			Metals

					_NA ×2

			Waters ×134

PDB id:

4z46

Links

Name:

Hydrolase

Title:

X-ray structure of the bis-platinum lysozyme adduct formed in the reaction between the protein and the two drugs cisplatin and oxaliplatin

Structure:

LysozymE C. Chain: a. Synonym: 1,4-beta-n-acetylmuramidasE C,allergen gal d iv. Ec: 3.2.1.17

Source:

Gallus gallus. Chicken. Organism_taxid: 9031

Resolution:

1.85Å

R-factor:

0.158

R-free:

0.218

Authors:

A.Merlino

Key ref:

D.Marasco et al. (2015). Oxaliplatin vs. cisplatin: competition experiments on their binding to lysozyme. Dalton Trans, 44, 10392-10398. PubMed id: 25974859 DOI: 10.1039/c5dt01279a

Date:

01-Apr-15

Release date:

27-May-15

PROCHECK

	Headers

	References

Protein chain

P00698 (LYSC_CHICK) - Lysozyme C from Gallus gallus

Seq: Struc:					147 a.a. 129 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.3.2.1.17 - lysozyme.

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

Reaction:

Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.

DOI no: 10.1039/c5dt01279a	Dalton Trans 44:10392-10398 (2015)
PubMed id: 25974859

Oxaliplatin vs. cisplatin: competition experiments on their binding to lysozyme.
D.Marasco, L.Messori, T.Marzo, A.Merlino.

ABSTRACT

The model protein hen egg white lysozyme was challenged with oxaliplatin and cisplatin. ESI mass spectrometry, surface plasmon resonance and thermal shift analyses demonstrate the formation of a bis-platinum adduct, though in very small amounts. Crystals of the bis-platinum adduct were obtained using two different preparations and the X-ray structures were solved at 1.85 Å and 1.95 Å resolution. Overall, the obtained data point out that, under the analyzed conditions, the two Pt drugs have similar affinities for the protein, but bind on its surface at two non-overlapping sites. In other words, these two drugs manifest a significantly different reactivity with this model protein and do not compete for the same protein binding sites.