2jpm: Difference between revisions
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jpm OCA], [http://www.ebi.ac.uk/pdbsum/2jpm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jpm RCSB]</span> | |||
}} | }} | ||
| Line 31: | Line 34: | ||
[[Category: peptide]] | [[Category: peptide]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:00:30 2008'' | ||
Revision as of 04:00, 31 March 2008
| |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Lactococcin G-b in TFE
OverviewOverview
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.
About this StructureAbout this Structure
2JPM is a Single protein structure of sequence from Lactococcus lactis. Full crystallographic 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
Page seeded by OCA on Mon Mar 31 04:00:30 2008