2cex
From Proteopedia
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'''STRUCTURE OF A SIALIC ACID BINDING PROTEIN (SIAP) IN THE PRESENCE OF THE SIALIC ACID ACID ANALOGUE NEU5AC2EN''' | '''STRUCTURE OF A SIALIC ACID BINDING PROTEIN (SIAP) IN THE PRESENCE OF THE SIALIC ACID ACID ANALOGUE NEU5AC2EN''' | ||
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[[Category: Wilkinson, A J.]] | [[Category: Wilkinson, A J.]] | ||
[[Category: Wilson, K S.]] | [[Category: Wilson, K S.]] | ||
| - | [[Category: | + | [[Category: Esr]] |
| - | [[Category: | + | [[Category: Neu5ac2en]] |
| - | [[Category: | + | [[Category: Periplasmic]] |
| - | [[Category: | + | [[Category: Periplasmic binding protein]] |
| - | [[Category: | + | [[Category: Sialic acid]] |
| - | [[Category: | + | [[Category: Transport]] |
| - | [[Category: | + | [[Category: Virulence factor]] |
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Revision as of 18:58, 3 May 2008
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 2,3-didehydro-2-deoxy-N-acetylneuraminic acid reveals the ligand bound in a deep cavity with its carboxylate group forming a salt bridge with a highly conserved Arg residue. Sialic acid binding, which obeys simple bimolecular association kinetics as determined by stopped-flow fluorescence spectroscopy, is accompanied by domain closure about a hinge region and the kinking of an alpha-helix hinge component. The structure provides insight into the evolution, mechanism, and substrate specificity of ESR-dependent secondary transporters that are widespread in prokaryotes.
About this Structure
2CEX is a Single protein structure of sequence from Haemophilus influenzae. 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 Page seeded by OCA on Sat May 3 21:58:07 2008
