PMID- 23225222 OWN - NLM STAT- MEDLINE DCOM- 20141112 LR - 20160518 IS - 1874-270X (Electronic) IS - 1874-270X (Linking) VI - 8 IP - 1 DP - 2014 Apr TI - Backbone resonance assignments of the outer membrane lipoprotein FrpD from Neisseria meningitidis. PG - 53-5 LID - 10.1007/s12104-012-9451-5 [doi] AB - The iron-regulated FrpD protein is a unique lipoprotein embedded into the outer membrane of the Gram-negative bacterium Neisseria meningitidis. The biological function of FrpD remains unknown but might consist in anchoring to the bacterial cell surface the Type I-secreted FrpC protein, which belongs to a Repeat in ToXins (RTX) protein family and binds FrpD with very high affinity (K(d) = 0.2 nM). Here, we report the backbone (1)H, (13)C, and (15)N chemical shift assignments for the FrpD(43-271) protein that allow us to characterize the intimate interaction between FrpD and the N-terminal domain of FrpC. FAU - Bumba, Ladislav AU - Bumba L AD - Institute of Microbiology of the ASCR, v.v.i., Videnska 1083, Prague, 142 20, Czech Republic. FAU - Sviridova, Ekaterina AU - Sviridova E FAU - Kuta Smatanova, Ivana AU - Kuta Smatanova I FAU - Rezacova, Pavlina AU - Rezacova P FAU - Veverka, Vaclav AU - Veverka V LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't DEP - 20121209 PL - Netherlands TA - Biomol NMR Assign JT - Biomolecular NMR assignments JID - 101472371 RN - 0 (Bacterial Outer Membrane Proteins) RN - 0 (Lipoproteins) SB - IM MH - Amino Acid Sequence MH - Bacterial Outer Membrane Proteins/*chemistry MH - Lipoproteins/*chemistry MH - Neisseria meningitidis/*metabolism MH - *Nuclear Magnetic Resonance, Biomolecular EDAT- 2012/12/12 06:00 MHDA- 2014/11/13 06:00 CRDT- 2012/12/11 06:00 PHST- 2012/10/11 00:00 [received] PHST- 2012/12/04 00:00 [accepted] PHST- 2012/12/11 06:00 [entrez] PHST- 2012/12/12 06:00 [pubmed] PHST- 2014/11/13 06:00 [medline] AID - 10.1007/s12104-012-9451-5 [doi] PST - ppublish SO - Biomol NMR Assign. 2014 Apr;8(1):53-5. doi: 10.1007/s12104-012-9451-5. Epub 2012 Dec 9.