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Probing dimerization and structural flexibility of mammalian lipoxygenases by small-angle X-ray scattering.

Abstract：

:Human lipoxygenases (LOXs) and their metabolites have a great impact on human homeostasis and are of interest for targeted drug design. This goal requires detailed knowledge of their structures and an understanding of structure-function relationship. At the moment, there are two complete crystal structures for mammalian LOX [rabbit 12/15LOX (r-12/15LOX) and human 5LOX (h-5LOX)] and a fragment of human 12LOX. The low-resolution structures in solution for various LOX isoforms have brought about controversial results. Here we explored the behavior of r-12/15LOX in aqueous solution under different conditions (salt and pH) by small-angle X-ray scattering (SAXS) and compared it with human platelet-type 12S-LOX (hp-12LOX) and h-5LOX. Thermodynamic calculations concerning the stability of molecular assemblies, thermal motion analysis [TLSMD (translation, libration, and screw rotation motion detection based on crystallographic temperature factor B(j))], and results of SAXS analyses brought about the following conclusions: (i) in contrast to its crystal structure, r-12/15LOX functions as a monomer that dominates in solution; (ii) it dimerizes at higher protein concentrations in the presence of salt and with increasing degree of motional freedom of the N-terminal PLAT domain, as suggested by the Y98,614→R double mutant; (iii) in aqueous solutions, hp-12LOX is stable as a dimer, in contrast to h-5LOX and r-12/15LOX, which are monomeric; and (iv) all three mammalian isozymes show a high level of flexibility not only for the PLAT domain but also for other subdomains of the catalytic part in TLS (translation, libration, and screw rotation) analysis and hp-12LOX in SAXS.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Shang W,Ivanov I,Svergun DI,Borbulevych OY,Aleem AM,Stehling S,Jankun J,Kühn H,Skrzypczak-Jankun E

doi

10.1016/j.jmb.2011.04.035

subject

Has Abstract

pub_date

2011-06-17 00:00:00

pages

654-68

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(11)00450-5

journal_volume

409

pub_type

杂志文章

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