Skip to main content

Crystallization and preliminary crystallographic analysis of a novel haemolytic lectin from the mushroom Laetiporus sulphureus

Buy Article:

$48.00 plus tax (Refund Policy)

Abstract:

The novel haemolytic lectin from the parasitic mushroom Laetiporus sulphureus (LSL) is a homotetramer (∼140 kDa) composed of subunits associated by non-covalent bonds. It exhibits haemagglutin­ation and haemolytic activities, both of which are inhibited by N-­acetyllactosamine. The structural similarity found between LSL and the bacterial pore-forming toxins mosquitocidal toxin (MTX2) from Bacillus sphaericus and α-toxin from Clostridium septicum points to a mechanism of biological action involving the formation of pores in the target membranes. LSL has been crystallized using the hanging-drop vapour-diffusion method at 291 K. Diffraction-quality hexagonal crystals have unit-cell parameters a = b = 101.8, c = 193.9 Å and belong to space group P6322. A 2.7 Å native data set was collected with an Rmerge of 9.2%.

Keywords: haemolytic lectin; pore-forming proteins; tetramer

Document Type: Research Article

DOI: http://dx.doi.org/10.1107/S0907444904007991

Publication date: June 1, 2004

bsc/ayd/2004/00000060/00000006/art00025
dcterms_title,dcterms_description,pub_keyword
6
5
20
40
5

Access Key

Free Content
Free content
New Content
New content
Open Access Content
Open access content
Subscribed Content
Subscribed content
Free Trial Content
Free trial content
Cookie Policy
X
Cookie Policy
ingentaconnect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more