2X3A

AsaP1 inactive mutant E294Q, an extracellular toxic zinc metalloendopeptidase

Summary for 2X3A

• Entry DOI: 10.2210/pdb2x3a/pdb
• Related: 2X3B 2X3C
• Descriptor: TOXIC EXTRACELLULAR ENDOPEPTIDASE, ZINC ION, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (6 entities in total)
• Functional Keywords: hydrolase
• Biological source: AEROMONAS SALMONICIDA SUBSP. ACHROMOGENES
• Total number of polymer chains: 1
• Total formula weight: 38018.56

Authors

Bogdanovic, X.,Palm, G.J.,Singh, R.K.,Hinrichs, W. (deposition date: 2010-01-22, release date: 2011-02-02, Last modification date: 2023-12-20)

Primary citation

Bogdanovic, X.,Palm, G.J.,Schwenteit, J.,Singh, R.K.,Gudmundsdottir, B.K.,Hinrichs, W.
Structural Evidence of Intramolecular Propeptide Inhibition of the Aspzincin Metalloendopeptidase Asap1.
FEBS Lett., 590:3280-, 2016

PubMed 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.

PubMed: 27528449
DOI: 10.1002/1873-3468.12356

Experimental method

X-RAY DIFFRACTION (2 Å)