2jpm: Difference between revisions

Revision as of 15:49, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2jpm.png

Template:STRUCTURE 2jpm

Lactococcin G-b in TFELactococcin G-b in TFE

Template:ABSTRACT PUBMED 18187052

About this StructureAbout this Structure

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

ReferenceReference

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

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-'''Lactococcin G-b in TFE'''
+===Lactococcin G-b in TFE===
-==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.
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+{{ABSTRACT_PUBMED_18187052}}
 ==About this Structure==
-JPM 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=2JPM OCA].
+JPM 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=2JPM OCA].
 ==Reference==
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 [[Category: Membrane bound]]
 [[Category: Peptide]]
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