This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1col

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1col.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1col.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1col| PDB=1col | SCENE= }}
{{STRUCTURE_1col| PDB=1col | SCENE= }}
-
'''REFINED STRUCTURE OF THE PORE-FORMING DOMAIN OF COLICIN A AT 2.4 ANGSTROMS RESOLUTION'''
+
===REFINED STRUCTURE OF THE PORE-FORMING DOMAIN OF COLICIN A AT 2.4 ANGSTROMS RESOLUTION===
-
==Overview==
+
<!--
-
The E1 subgroup (E1, A, B, IA, IB, K and N) of anti-bacterial toxins called colicins is known to form voltage-dependent channels in lipid bilayers. The crystal structure of the pore-forming domain of colicin A from Escherichia coli has been refined to the diffraction limit of the crystals at 2.4 A resolution by means of molecular dynamics and restrained least-squares methods to a conventional R-factor of 0.18 for all data between 6.0 and 2.4 A resolution. The polypeptide chain of 204 amino acid residues consists of ten alpha-helices organized in a three-layer structure. The helices range in length from 9 to 23 residues with an average length of 125 residues. The packing arrangement of the helices has been analysed; the packing is different from that observed in four-helix bundle proteins. The sites of 83 water molecules have been located and refined. Analysis of the structure provides insights into the mechanism of formation of a voltage-gated channel by the protein. Although it is proposed that substantial tertiary structural changes occur during membrane insertion, the secondary structural elements remain conserved. This idea has been proposed recently for a number of other protein-membrane events and thus may have more general applicability.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1373773}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1373773 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1373773}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Tucker, A D.]]
[[Category: Tucker, A D.]]
[[Category: Antibacterial protein]]
[[Category: Antibacterial protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:57:06 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:01:38 2008''

Revision as of 18:01, 30 June 2008

Image:1col.png

Template:STRUCTURE 1col

REFINED STRUCTURE OF THE PORE-FORMING DOMAIN OF COLICIN A AT 2.4 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1373773

About this Structure

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

Reference

Refined structure of the pore-forming domain of colicin A at 2.4 A resolution., Parker MW, Postma JP, Pattus F, Tucker AD, Tsernoglou D, J Mol Biol. 1992 Apr 5;224(3):639-57. PMID:1373773

Page seeded by OCA on Mon Jun 30 21:01:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1col"
Personal tools