1etn: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1etn.gif|left|200px]]
{{Seed}}
[[Image:1etn.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1etn|  PDB=1etn  |  SCENE=  }}  
{{STRUCTURE_1etn|  PDB=1etn  |  SCENE=  }}  


'''MOLECULAR STRUCTURE OF THE TOXIC DOMAIN OF HEAT-STABLE ENTEROTOXIN PRODUCED BY A PATHOGENIC STRAIN OF ESCHERICHIA COLI'''
===MOLECULAR STRUCTURE OF THE TOXIC DOMAIN OF HEAT-STABLE ENTEROTOXIN PRODUCED BY A PATHOGENIC STRAIN OF ESCHERICHIA COLI===




==Overview==
<!--
Heat-stable enterotoxins are a family of toxin peptides that are produced by enterotoxigenic Escherichia coli and consist of 18 and 19 amino acid residues (Aimoto, S., Takao, T., Shimonishi, Y., Hara, S., Takeda, T., Takeda, Y., and Miwatani, T. (1982) Eur. J. Biochem. 129, 257-263). A synthetic fully toxic analog of the enterotoxin, Mpr5-STp(5-17), where Mpr is beta-mercaptopropionic acid and which consists of 13 amino acid residues from Cys5 to Cys17 in a heat-stable enterotoxin but is deaminated at its N terminus (Kubota, H., Hidaka, Y., Ozaki, H., Ito, H., Hirayama, T., Takeda, Y., and Shimonishi, Y. (1989) Biochem. Biophys. Res. Commun. 161, 229-235), has been crystalized from water, and its crystal structure has been solved by a direct method and refined by least square procedures to give an R factor of 0.089. The crystal belongs to the orthorhombic space group P2(1)2(1)2(1) with unit cell constants a = 21.010 (2) A, b = 27.621 (4) A, and c = 12.781 (1) A. The asymmetric unit of the crystals contains one peptide molecule with 13 water molecules. A right-hand spiral peptide backbone extends throughout the molecule. Three beta-turns are located along this spiral and fixed tightly by three intramolecular disulfide linkages. The actual structure predicts the biniding region on the enterotoxin to the receptor protein on the membrane of rat intestinal epithelial cells.
The line below this paragraph, {{ABSTRACT_PUBMED_2005130}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 2005130 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_2005130}}


==About this Structure==
==About this Structure==
Line 24: Line 28:
[[Category: Shimonishi, Y.]]
[[Category: Shimonishi, Y.]]
[[Category: Enterotoxin]]
[[Category: Enterotoxin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:30:25 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:57:57 2008''

Revision as of 22:57, 30 June 2008

File:1etn.png

Template:STRUCTURE 1etn

MOLECULAR STRUCTURE OF THE TOXIC DOMAIN OF HEAT-STABLE ENTEROTOXIN PRODUCED BY A PATHOGENIC STRAIN OF ESCHERICHIA COLI

Template:ABSTRACT PUBMED 2005130

About this Structure

1ETN is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Molecular structure of the toxin domain of heat-stable enterotoxin produced by a pathogenic strain of Escherichia coli. A putative binding site for a binding protein on rat intestinal epithelial cell membranes., Ozaki H, Sato T, Kubota H, Hata Y, Katsube Y, Shimonishi Y, J Biol Chem. 1991 Mar 25;266(9):5934-41. PMID:2005130

Page seeded by OCA on Tue Jul 1 01:57:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1etn&oldid=594010"