1w0o

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1w0o, resolution 1.9Å

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VIBRIO CHOLERAE SIALIDASE

Overview

Vibrio cholerae neuraminidase (VCNA) plays a significant role in the, pathogenesis of cholera by removing sialic acid from higher order, gangliosides to unmask GM1, the receptor for cholera toxin. We previously, showed that the structure of VCNA is composed of a central beta-propeller, catalytic domain flanked by two lectin-like domains; however the nature of, the carbohydrates recognized by these lectin domains has remained unknown., We present here structures of the enzyme in complex with two substrates, alpha-2,3-sialyllactose and alpha-2,6-sialyllactose. Both substrate, complexes reveal the alpha-anomer of N-acetylneuraminic acid (Neu5Ac), bound to the N-terminal lectin domain, thereby revealing the role of this, domain. The large number of interactions suggest a relatively high ... [(full description)]

About this Structure

1W0O is a [Single protein] structure of sequence from [Vibrio cholerae] with SIA, CA and DAN as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Sialic acid recognition by Vibrio cholerae neuraminidase., Moustafa I, Connaris H, Taylor M, Zaitsev V, Wilson JC, Kiefel MJ, von Itzstein M, Taylor G, J Biol Chem. 2004 Sep 24;279(39):40819-26. Epub 2004 Jun 28. PMID:15226294

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