PDBsum entry 2x3a

Hydrolase

PDB id: 2x3a

Contents

Protein chain

293 a.a. *

Ligands

MES

SO4 ×3

GOL ×2

Metals

_ZN

Waters ×199

* Residue conservation analysis

PDB id:

2x3a

Name:

Hydrolase

Title:

Asap1 inactive mutant e294q, an extracellular toxic zinc metalloendopeptidase

Structure:

Toxic extracellular endopeptidase. Chain: a. Engineered: yes. Mutation: yes

Source:

Aeromonas salmonicida subsp. Achromogenes. Organism_taxid: 113288. Strain: keldur265-87. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.172 R-free: 0.205

Authors:

X.Bogdanovic,G.J.Palm,R.K.Singh,W.Hinrichs

Key ref:

X.Bogdanović et al. (2016). Structural evidence of intramolecular propeptide inhibition of the aspzincin metalloendopeptidase AsaP1. Febs Lett, 590, 3280-3294. PubMed id: 27528449 DOI: 10.1002/1873-3468.12356

Date:

22-Jan-10 Release date: 02-Feb-11

Protein chain

Q8GMV9  (Q8GMV9_AERSA) -  Toxic extracellular endopeptidase from Aeromonas salmonicida subsp. achromogenes

Seq: 343 a.a.

Struc: 293 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.3.4.24.39 - deuterolysin.
• Reaction: Preferential cleavage of bonds with hydrophobic residues in P1'; also 3-Asn-|-Gln-4 and 8-Gln-|-Ser-9 bonds in insulin B chain.
• Cofactor: Zn(2+)

DOI no: 10.1002/1873-3468.12356

Febs Lett 590:3280-3294 (2016)

PubMed id: 27528449

Structural evidence of intramolecular propeptide inhibition of the aspzincin metalloendopeptidase AsaP1.

X.Bogdanović, G.J.Palm, J.Schwenteit, R.K.Singh, B.K.Gudmundsdóttir, W.Hinrichs.

ABSTRACT

The Gram-negative bacterium Aeromonas salmonicida is a fish pathogen for various fish species worldwide. Aeromonas salmonicida subsp. achromogenes produces the extracellular, toxic zinc endopeptidase AsaP1. Crystal structure analyses at 2.0 Å resolution of two proteolytically inactive AsaP1 variants show the polypeptide folding of the protease domain and the propeptide domain. These first crystal structure analyses of a precursor of a deuterolysin-like aspzincin protease provide insights into propeptide function, and specific substrate binding. A lysine side chain of the propeptide binds in the hydrophobic S1'-pocket interacting with three carboxylate side chains. An AsaP1 variant with a lysine to alanine exchange identifies the chaperone function of the propeptide.