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1r9l

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[[Image:1r9l.gif|left|200px]]
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{{STRUCTURE_1r9l| PDB=1r9l | SCENE= }}
{{STRUCTURE_1r9l| PDB=1r9l | SCENE= }}
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'''structure analysis of ProX in complex with glycine betaine'''
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===structure analysis of ProX in complex with glycine betaine===
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==Overview==
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Compatible solutes such as glycine betaine and proline betaine are accumulated to exceedingly high intracellular levels by many organisms in response to high osmolarity to offset the loss of cell water. They are excluded from the immediate hydration shell of proteins and thereby stabilize their native structure. Despite their exclusion from protein surfaces, the periplasmic ligand-binding protein ProX from the Escherichia coli ATP-binding cassette transport system ProU binds the compatible solutes glycine betaine and proline betaine with high affinity and specificity. To understand the mechanism of compatible solute binding, we determined the high resolution structure of ProX in complex with its ligands glycine betaine and proline betaine. This crystallographic study revealed that cation-pi interactions between the positive charge of the quaternary amine of the ligands and three tryptophan residues forming a rectangular aromatic box are the key determinants of the high affinity binding of compatible solutes by ProX. The structural analysis was combined with site-directed mutagenesis of the ligand binding pocket to estimate the contributions of the tryptophan residues involved in binding.
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The line below this paragraph, {{ABSTRACT_PUBMED_14612446}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 14612446 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14612446}}
==About this Structure==
==About this Structure==
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[[Category: Periplasmic binding protein]]
[[Category: Periplasmic binding protein]]
[[Category: Tryptophan box]]
[[Category: Tryptophan box]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:14:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:05:45 2008''

Revision as of 01:05, 28 July 2008

Image:1r9l.png

Template:STRUCTURE 1r9l

structure analysis of ProX in complex with glycine betaine

Template:ABSTRACT PUBMED 14612446

About this Structure

1R9L is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Cation-pi interactions as determinants for binding of the compatible solutes glycine betaine and proline betaine by the periplasmic ligand-binding protein ProX from Escherichia coli., Schiefner A, Breed J, Bosser L, Kneip S, Gade J, Holtmann G, Diederichs K, Welte W, Bremer E, J Biol Chem. 2004 Feb 13;279(7):5588-96. Epub 2003 Nov 11. PMID:14612446

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