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| - | [[Image:1ehs.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ehs| PDB=1ehs | SCENE= }} | | {{STRUCTURE_1ehs| PDB=1ehs | SCENE= }} |
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| - | '''THE STRUCTURE OF ESCHERICHIA COLI HEAT-STABLE ENTEROTOXIN B BY NUCLEAR MAGNETIC RESONANCE AND CIRCULAR DICHROISM'''
| + | ===THE STRUCTURE OF ESCHERICHIA COLI HEAT-STABLE ENTEROTOXIN B BY NUCLEAR MAGNETIC RESONANCE AND CIRCULAR DICHROISM=== |
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| - | ==Overview==
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| - | The heat-stable enterotoxin b (STb) is secreted by enterotoxigenic Escherichia coli that cause secretory diarrhea in animals and humans. It is a 48-amino acid peptide containing two disulfide bridges, between residues 10 and 48 and 21 and 36, which are crucial for its biological activity. Here, we report the solution structure of STb determined by two- and three-dimensional NMR methods. Approximate interproton distances derived from NOE data were used to construct structures of STb using distance-geometry and simulated annealing procedures. The NMR-derived structure shows that STb is helical between residues 10 and 22 and residues 38 and 44. The helical structure in the region 10-22 is amphipathic and exposes several polar residues to the solvent, some of which have been shown to be important in determining the toxicity of STb. The hydrophobic residues on the opposite face of this helix make contacts with the hydrophobic residues of the C-terminal helix. The loop region between residues 21 and 36 has another cluster of hydrophobic residues and exposes Arg 29 and Asp 30, which have been shown to be important for intestinal secretory activity. CD studies show that reduction of disulfide bridges results in a dramatic loss of structure, which correlates with loss of function. Reduced STb adopts a predominantly random-coil conformation. Chromatographic measurements of concentrations of native, fully reduced, and single-disulfide species in equilibrium mixtures of STb in redox buffers indicate that the formation of the two disulfide bonds in STb is only moderately cooperative. Similar measurements in the presence of 8 M urea suggest that the native secondary structure significantly stabilizes the disulfide bonds. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8528070}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8528070 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8528070}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1EHS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHS OCA]. | + | 1EHS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHS OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Enterotoxin]] | | [[Category: Enterotoxin]] |
| | [[Category: Heat-stable]] | | [[Category: Heat-stable]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:07:02 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:42:58 2008'' |
Revision as of 21:43, 30 June 2008
Template:STRUCTURE 1ehs
THE STRUCTURE OF ESCHERICHIA COLI HEAT-STABLE ENTEROTOXIN B BY NUCLEAR MAGNETIC RESONANCE AND CIRCULAR DICHROISM
Template:ABSTRACT PUBMED 8528070
About this Structure
1EHS is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.
Reference
The structure of Escherichia coli heat-stable enterotoxin b by nuclear magnetic resonance and circular dichroism., Sukumar M, Rizo J, Wall M, Dreyfus LA, Kupersztoch YM, Gierasch LM, Protein Sci. 1995 Sep;4(9):1718-29. PMID:8528070
Page seeded by OCA on Tue Jul 1 00:42:58 2008
