Low-resolution molecular structures of isolated functional units from arthropodan and molluscan hemocyanin.

Abstract:

:Synchrotron x-ray scattering measurements were performed on dilute solutions of the purified hemocyanin subunit (Bsin1) from scorpion (Buthus sindicus) and the N-terminal functional unit (Rta) from a marine snail (Rapana thomasiana). The model-independent approach based on spherical harmonics was applied to calculate the molecular envelopes directly from the scattering profiles. Their molecular shapes in solution could be restored at 2-nm resolution. We show that these units represent stable, globular building blocks of the two hemocyanin families and emphasize their conformational differences on a subunit level. Because no crystallographic or electron microscopy data are available for isolated functional units, this study provides for the first time structural information for isolated, monomeric functional subunits from both hemocyanin families. This has been made possible through the use of low protein concentrations (< or = 1 mg/ml). The observed structural differences may offer advantages in building very different overall molecular architectures of hemocyanin by the two phyla.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Grossmann JG,Ali SA,Abbasi A,Zaidi ZH,Stoeva S,Voelter W,Hasnain SS

doi

10.1016/s0006-3495(00)76655-0

subject

Has Abstract

pub_date

2000-02-01 00:00:00

pages

977-81

issue

2

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(00)76655-0

journal_volume

78

pub_type

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