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==ASAP1 INACTIVE MUTANT E294Q, AN EXTRACELLULAR TOXIC ZINC METALLOENDOPEPTIDASE==
==AsaP1 inactive mutant E294Q, an extracellular toxic zinc metalloendopeptidase==
<StructureSection load='2x3a' size='340' side='right' caption='[[2x3a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2x3a' size='340' side='right' caption='[[2x3a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Two mutants of the toxic extracellular zinc endopeptidase AsaP1 (AsaP1_E294Q and AsaP1_E294A) of Aeromonas salmonicida subsp. achromogenes were expressed in Escherichia coli and crystallized by the vapour-diffusion method. Crystals were obtained using several precipitants and different protein concentrations. Protein crystals were found in a monoclinic (C2) as well as an orthorhombic (P2(1)2(1)2(1)) space group. The crystals belonging to the monoclinic space group C2 had unit-cell parameters a = 103.4, b = 70.9, c = 54.9 A, beta = 109.3 degrees for AsaP1_E294A, and a = 98.5, b = 74.5, c = 54.7 A, beta = 112.4 degrees for AsaP1_E294Q. The unit-cell parameters of the orthorhombic crystal obtained for AsaP1_E294A were a = 57.9, b = 60.2, c = 183.6 A. The crystals of the two different mutants diffracted X-rays beyond 2.0 A resolution.
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.


Crystallization and preliminary X-ray diffraction studies of AsaP1_E294A and AsaP1_E294Q, two inactive mutants of the toxic zinc metallopeptidase AsaP1 from Aeromonas salmonicida subsp. achromogenes.,Bogdanovic X, Singh RK, Hentschke J, Gudmundsdottir BK, Hinrichs W Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jul 1;65(Pt, 7):695-7. Epub 2009 Jun 27. PMID:19574642<ref>PMID:19574642</ref>
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<ref>PMID:27528449</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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