BMRB Entry 20032

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR20032

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Title:
Solution structure of Gelatinase Biosynthesis-Activating Pheromone (GBAP), a 11-residue peptide lactone, from the Gram-positive bacterium Enterococcus faecalis
Deposition date:
2008-07-16
Original release date:
2009-04-04
Authors:
Nagata, Koji; Nishiguchi, Kenzo; Kameda, Yasuhiro; Sonomoto, Kenji; Nakayama, Jiro; Tanokura, Masaru
Citation:

Citation: Nishiguchi, Kenzo; Nagata, Koji; Tanokura, Masaru; Sonomoto, Kenji; Nakayama, Jiro. "Structure-Activity Relationship of Gelatinase Biosynthesis-Activating Pheromone of Enterococcus faecalis"  J. Bacteriol. 191, 641-650 (2009).
PubMed: 18996993

Assembly members:

Assembly members:
GBAP, polymer, 11 residues, 1303.470 Da.

Natural source:

Natural source:   Common Name: Enterococcus faecalis   Taxonomy ID: 1351   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Enterococcus faecalis

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GBAP: QNSPNIFGQWM

Data sets:
Data typeCount
15N chemical shifts10
1H chemical shifts60

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Assembly:

Entity Assembly IDEntity NameEntity ID
1GBAP1

Entities:

Entity 1, GBAP 11 residues - 1303.470 Da.

GBAP consists of 11 amino acid residues with a lactone linkage between the alpha-carboxyl group at the C-terminal Met11 and the gamma-hydroxyl group of Ser3.

1   GLNASNSERPROASNILEPHEGLYGLNTRP
2   MET

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