2x3b

AsaP1 inactive mutant E294A, an extracellular toxic zinc metalloendopeptidase

spinqualitylabelsall models 2x3b, resolution 2.28Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2x3b is a 2 chain structure with sequence from "necromonas_achromogenes"_smith_1963 "necromonas achromogenes" smith 1963. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Related: 2x3c, 2x3a Activity: Deuterolysin, with EC number 3.4.24.39 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 A 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. Structural evidence of intramolecular propeptide inhibition of the aspzincin metalloendopeptidase AsaP1.,Bogdanovic X, Palm GJ, Schwenteit J, Singh RK, Gudmundsdottir BK, Hinrichs W FEBS Lett. 2016 Aug 16. doi: 10.1002/1873-3468.12356. PMID:27528449 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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