Structural highlights
2x3c is a 1 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.
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| Ligands: | , , , |
| Related: | 2x3b, 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bogdanovic X, Palm GJ, Schwenteit J, Singh RK, Gudmundsdottir BK, Hinrichs W. Structural evidence of intramolecular propeptide inhibition of the aspzincin metalloendopeptidase AsaP1. FEBS Lett. 2016 Aug 16. doi: 10.1002/1873-3468.12356. PMID:27528449 doi:http://dx.doi.org/10.1002/1873-3468.12356
