PDBsum entry 2n93

Lipid binding protein

PDB id: 2n93

Contents

Protein chain

130 a.a.

PDB id:

2n93

Name:

Lipid binding protein

Title:

Solution structure of lcfabp

Structure:

Fatty acid-binding protein. Chain: a. Synonym: lcfabp. Engineered: yes

Source:

Luciola cerata. Organism_taxid: 1071519. Gene: fabp. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

10 models

Authors:

K.Tseng,P.Lyu

Key ref:

K.L.Tseng et al. (2016). 1H, 15N and 13C resonance assignments of light organ-associated fatty acid-binding protein of Taiwanese fireflies. Biomol Nmr Assign, 10, 71-74. PubMed id: 26373428 DOI: 10.1007/s12104-015-9640-0

Date:

05-Nov-15 Release date: 20-Jan-16

Protein chain

G1FKW0  (G1FKW0_9COLE) -  Fatty acid-binding protein from Abscondita cerata

Seq: 130 a.a.

Struc: 130 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1007/s12104-015-9640-0

Biomol Nmr Assign 10:71-74 (2016)

PubMed id: 26373428

1H, 15N and 13C resonance assignments of light organ-associated fatty acid-binding protein of Taiwanese fireflies.

K.L.Tseng, Y.Z.Lee, Y.R.Chen, P.C.Lyu.

ABSTRACT

Fatty acid-binding proteins (FABPs) are a family of proteins that modulate the transfer of various fatty acids in the cytosol and constitute a significant portion in many energy-consuming cells. The ligand binding properties and specific functions of a particular type of FABP seem to be diverse and depend on the respective binding cavity as well as the cell type from which this protein is derived. Previously, a novel FABP (lcFABP; lc: Luciola cerata) was identified in the light organ of Taiwanese fireflies. The lcFABP was proved to possess fatty acids binding capabilities, especially for fatty acids of length C14-C18. However, the structural details are unknown, and the structure-function relationship has remained to be further investigated. In this study, we finished the (1)H, (15)N and (13)C chemical shift assignments of (15)N/(13)C-enriched lcFABP by solution NMR spectroscopy. In addition, the secondary structure distribution was revealed based on the backbone N, H, Cα, Hα, C and side chain Cβ assignments. These results can provide the basis for further structural exploration of lcFABP.