2cex

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spinqualitylabelsall models 2cex, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF A SIALIC ACID BINDING PROTEIN (SIAP) IN THE PRESENCE OF THE SIALIC ACID ACID ANALOGUE NEU5AC2EN

Overview

Extracytoplasmic solute receptors (ESRs) are important components of, solute uptake systems in bacteria, having been studied extensively as, parts of ATP binding cassette transporters. Herein we report the first, crystal structure of an ESR protein from a functionally characterized, electrochemical ion gradient dependent secondary transporter. This, protein, SiaP, forms part of a tripartite ATP-independent periplasmic, transporter specific for sialic acid in Haemophilus influenzae., Surprisingly, the structure reveals an overall topology similar to ATP, binding cassette ESR proteins, which is not apparent from the sequence, demonstrating that primary and secondary transporters can share a common, structural component. The structure of SiaP in the presence of the sialic, acid analogue ... [(full description)]

About this Structure

2CEX is a [Single protein] structure of sequence from [Haemophilus influenzae] with ZN, DAN and GOL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Conservation of structure and mechanism in primary and secondary transporters exemplified by SiaP, a sialic acid binding virulence factor from Haemophilus influenzae., Muller A, Severi E, Mulligan C, Watts AG, Kelly DJ, Wilson KS, Wilkinson AJ, Thomas GH, J Biol Chem. 2006 Aug 4;281(31):22212-22. Epub 2006 May 15. PMID:16702222

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