title: Crystallization and preliminary analysis of neurolysin.
abstract: Neuropeptidases inactivate or modify the activity of peptide neurotransmitters and neurohormones. The neuropeptidase neurolysin acts only on short peptides and accepts a variety of cleavage-site sequences. Structures of the enzyme and enzyme-substrate complexes will help to determine the mechanisms of substrate selectivity used by this enzyme. Crystals of recombinant neurolysin have been grown in the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 157.8, b = 88.0, c = 58.4 A. Data have been collected to 2.3 A at 110 K with observed diffraction to 1.8 A. Circular dichroism measurements suggest that the enzyme is primarily alpha-helical, with little beta-strand secondary structure. Sequence-based secondary-structure prediction supports this conclusion.
authors.affiliation: Department of Biochemistry and Center for Structural Biology, University of Kentucky, Lexington, Kentucky 40536, USA.
authors.forename: W
authors.initials: W
authors.lastname: Lian
authors.forename: G
authors.initials: G
authors.lastname: Chen
authors.forename: D
authors.initials: D
authors.lastname: Wu
authors.forename: C K
authors.initials: CK
authors.lastname: Brown
authors.forename: K
authors.initials: K
authors.lastname: Madauss
authors.forename: L B
authors.initials: LB
authors.lastname: Hersh
authors.forename: D W
authors.initials: DW
authors.lastname: Rodgers
mesh_terms: D000818:Animals; D002942:Circular Dichroism; D003460:Crystallization; D004926:Escherichia coli; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017433:Protein Structure, Secondary; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D014961:X-Ray Diffraction
chemical_list: D011994:Recombinant Proteins; D008666:Metalloendopeptidases; C062316:neurolysin