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.


2jpj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2jpj.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2jpj.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2jpj| PDB=2jpj | SCENE= }}
{{STRUCTURE_2jpj| PDB=2jpj | SCENE= }}
-
'''Lactococcin G-a in DPC'''
+
===Lactococcin G-a in DPC===
-
==Overview==
+
<!--
-
The three-dimensional structures of the two peptides, lactococcin G-alpha (LcnG-alpha; contains 39 residues) and lactococcin G-beta (LcnG-beta, contains 35 residues), that constitute the two-peptide bacteriocin lactococcin G (LcnG) have been determined by nuclear magnetic resonance (NMR) spectroscopy in the presence of DPC micelles and TFE. In DPC, LcnG-alpha has an N-terminal alpha-helix (residues 3-21) that contains a GxxxG helix-helix interaction motif (residues 7-11) and a less well defined C-terminal alpha-helix (residues 24-34), and in between (residues 18-22) there is a second somewhat flexible GxxxG-motif. Its structure in TFE was similar. In DPC, LcnG-beta has an N-terminal alpha-helix (residues 6-19). The region from residues 20 to 35, which also contains a flexible GxxxG-motif (residues 18-22), appeared to be fairly unstructured in DPC. In the presence of TFE, however, the region between and including residues 23 and 32 formed a well defined alpha-helix. The N-terminal helix between and including residues 6 and 19 seen in the presence of DPC, was broken at residues 8 and 9 in the presence of TFE. The N-terminal helices, both in LcnG-alpha and -beta, are amphiphilic. We postulate that LcnG-alpha and -beta have a parallel orientation and interact through helix-helix interactions involving the first GxxxG (residues 7-11) motif in LcnG-alpha and the one (residues 18-22) in LcnG-beta, and that they thus lie in a staggered fashion relative to each other.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18187052}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18187052 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18187052}}
==About this Structure==
==About this Structure==
-
2JPJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JPJ OCA].
+
2JPJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JPJ OCA].
==Reference==
==Reference==
Line 30: Line 34:
[[Category: Membrane bound]]
[[Category: Membrane bound]]
[[Category: Peptide]]
[[Category: Peptide]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:09:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:44:14 2008''

Revision as of 09:44, 27 July 2008

Image:2jpj.png

Template:STRUCTURE 2jpj

Lactococcin G-a in DPC

Template:ABSTRACT PUBMED 18187052

About this Structure

2JPJ is a Single protein structure of sequence from Lactococcus lactis. Full experimental information is available from OCA.

Reference

Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin lactococcin G., Rogne P, Fimland G, Nissen-Meyer J, Kristiansen PE, Biochim Biophys Acta. 2007 Dec 15;. PMID:18187052

Page seeded by OCA on Sun Jul 27 12:44:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jpj"
Personal tools