The 17A structure of the 420 kDa lobster clottable protein by single particle reconstruction from cryoelectron micrographs.

Abstract:

:Crustaceans form clots by the rapid crosslinking of a hemolymph clottable protein (CP) to form long, branched polymers. Clotting limits hemolymph loss from wounds as well as playing a part in the innate immune response. CP is a 420 kDa homodimer with a large quantity of associated lipid, primarily the carotenoid pigment astaxanthin. The three-dimensional structure of CP from the lobster Panulirus interruptus has been determined to 17 A resolution by single particle reconstruction from electron micrographs of the protein embedded in vitreous ice. The most prominent feature of this structure is a large cavity spanning the length of the molecule, which is the likely lipid binding pocket. The EM structure has been used in a low resolution molecular replacement search with data from orthorhombic CP crystals, and a solution is presented which describes the crystal packing.

journal_name

J Struct Biol

authors

Kollman JM,Quispe J

doi

10.1016/j.jsb.2005.06.008

keywords:

subject

Has Abstract

pub_date

2005-09-01 00:00:00

pages

306-14

issue

3

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(05)00132-2

journal_volume

151

pub_type

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