ISDA: 2X3B

Deposition Date 2010-01-22

Release Date 2011-02-02

Last Version Date 2024-11-13

Entry Detail

PDB ID:

2X3B

Keywords:

HYDROLASE

Title:

AsaP1 inactive mutant E294A, an extracellular toxic zinc metalloendopeptidase

Biological Source:

Source Organism(s):

AEROMONAS SALMONICIDA SUBSP. ACHROMOGENES (Taxon ID: 113288)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.28 Å

R-Value Free:

0.29

R-Value Work:

0.24

R-Value Observed:

0.24

Space Group:

P 21 21 21

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:TOXIC EXTRACELLULAR ENDOPEPTI
Gene (Uniprot):asaP1
Mutagens:YES
Chain IDs:A, B
Chain Length:343
Number of Molecules:2
Biological Source:AEROMONAS SALMONICIDA SUBSP. ACHROMOGENES

UniProt ID:Q8GMV9 Pfam ID:PF14521 EC:3.4.24.39

Ligand Molecules

Primary Citation

Structural Evidence of Intramolecular Propeptide Inhibition of the Aspzincin Metalloendopeptidase Asap1.

Bogdanovic, X, Palm, G.J, Schwenteit, J, Singh, R.K, Gudmundsdottir, B.K, Hinrichs, W.Show

FEBS Lett. 590 3280 ? (2016)

PMID: 27528449 DOI: 10.1002/1873-3468.12356

Abstact

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.

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Protein

Chemical

Disease

Primary Citation of related structures

Abstact

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