2cey

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{{STRUCTURE_2cey| PDB=2cey | SCENE= }}
{{STRUCTURE_2cey| PDB=2cey | SCENE= }}
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'''APO STRUCTURE OF SIAP'''
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===APO STRUCTURE OF SIAP===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16702222 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16702222}}
==About this Structure==
==About this Structure==
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[[Category: Transport]]
[[Category: Transport]]
[[Category: Virulence factor]]
[[Category: Virulence factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:52:30 2008''

Revision as of 20:52, 27 July 2008

Image:2cey.png

Template:STRUCTURE 2cey

APO STRUCTURE OF SIAP

Template:ABSTRACT PUBMED 16702222

About this Structure

2CEY 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

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