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Document Page 465 80 × 40 Å with a narrow centrally attached stalk (15 Å wide and 100 Å long), which terminates into a hydrophobic knob anchored in the viral envelope. The detergent-released spikes can be digested by pronase to release the neuraminidase “heads,” which retain full antigenic and enzyme activity [40,41]. The molecule was found to be a tetramer of molecular weight 240,000, reducing to 200,000 when treated with pronase [42]. A low resolution x-ray image of crystallized neuraminidase heads [43] established that the enzyme had circular 4-fold symmetry. III. Molecular Structure of Neuraminidase Crystals of pronase-released heads of the N2 human strains of A/Tokyo/3/67 [44] and A/RI/5+/57 were used for an x-ray structure determination. The x-ray 3-dimensional molecular structure of neuraminidase heads was determined [45] for these two N2 subtypes by a novel technique of molecular electron density averaging from two different crystal systems, using a combination of multiple isomorphous replacement and noncrystallographic symmetry averaging. The structure of A/Tokyo/3/67 N2 has been refined [46] to 2.2 Å as has the structures of two avian N9 subtypes [47–49]. Three influenza type B structures [50] have also been determined and found to have an identical fold with 60 residues (including 16 conserved cysteine residues) being invariant. Bacterial sialidases from salmonella [51] and cholera [52] have homologous structures to influenza neuraminidase, but few of the residues are structurally invariant. A. Structural Topology The protein fold consists of a symmetric arrangement of six four-stranded antiparallel β sheets arrange as blades of a propeller (Figure 3), the propeller axis being approximately parallel to but titled away from the circular 4-fold axis of the tetramer. This tilt angle varies between the known subtypes. This topology has now also been found in the seven β sheet propeller structure of bacterial methylamine dehydrogenase [53] and galactose oxidase [54], and the eight β sheet propeller structure of methanol dehydrogenase [55]. Each sheet of neuraminidase has a “W” topology (+1,+1,+1) [56] with four strands connected by reverse turns (Figure 3). The first strand of each sheet enters from the top, approximately parallel to and near the propeller axis; the fourth strand exits from the bottom, approximately perpendicular to the propeller axis. Top and bottom surfaces of the head refer to the faces of the tetramer away and towards the viral membrane respectively. Each sheet thus has a characteristic 90° right-hand twist between the inner- and outermost strand. The six sheets and their connections to each other are topologically identical. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_465.html [4/9/2004 12:13:21 AM]
Document Figure 3 (a) A MOLSCRIPT [107] stereo diagram of the neuraminidase tetramer viewed from above down the symmetry axis. The different shaded arrows represent β strands comprising the six β sheets that form the “propeller” framework of each subunit. (b) A stereo diagram of a neuraminidase monomer viewed down the 4-fold axis, and α-sialic acid is shown bound in the active site of the enzyme, which lies in a pocket formed by the six β sheets near the pseudo six-fold axis of each subunit. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_466.html (1 of 2) [4/9/2004 12:15:39 AM] Page 466
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