Crystallization and preliminary analysis of neurolysin.
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.
Lian
W
W
Department of Biochemistry and Center for Structural Biology, University of Kentucky, Lexington, Kentucky 40536, USA.
Chen
G
G
Wu
D
D
Brown
C K
CK
Madauss
K
K
Hersh
L B
LB
Rodgers
D W
DW
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
D011994:Recombinant Proteins; D008666:Metalloendopeptidases; C062316:neurolysin