2cex
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | Extracytoplasmic solute receptors (ESRs) are important components of | + | 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== | ==About this Structure== | ||
| Line 13: | Line 13: | ||
[[Category: Haemophilus influenzae]] | [[Category: Haemophilus influenzae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kelly, D | + | [[Category: Kelly, D J.]] |
[[Category: Muller, A.]] | [[Category: Muller, A.]] | ||
[[Category: Mulligan, C.]] | [[Category: Mulligan, C.]] | ||
[[Category: Severi, E.]] | [[Category: Severi, E.]] | ||
| - | [[Category: Thomas, G | + | [[Category: Thomas, G H.]] |
| - | [[Category: Watts, A | + | [[Category: Watts, A G.]] |
| - | [[Category: Wilkinson, A | + | [[Category: Wilkinson, A J.]] |
| - | [[Category: Wilson, K | + | [[Category: Wilson, K S.]] |
[[Category: DAN]] | [[Category: DAN]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
| Line 33: | Line 33: | ||
[[Category: virulence factor]] | [[Category: virulence factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:47:54 2008'' |
Revision as of 14:47, 21 February 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 with , and as ligands. Known structural/functional Site: . 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 Thu Feb 21 16:47:54 2008
Categories: Haemophilus influenzae | Single protein | Kelly, D J. | Muller, A. | Mulligan, C. | Severi, E. | Thomas, G H. | Watts, A G. | Wilkinson, A J. | Wilson, K S. | DAN | GOL | ZN | Esr | Neu5ac2en | Periplasmic | Periplasmic binding protein | Sialic acid | Transport | Tripartite atp-independent periplasmic (trap)transport | Virulence factor
