Background

The crystal structure of a periplasmic l-aspartate/l-glutamate binding protein (DEBP) from Shigella flexneri complexed with an l-glutamate molecule has been determined and refined to an atomic resolution of 1.0 A. There are two DEBP molecules in the asymmetric unit. The refined model contains 4462 non-hydrogen protein atoms, 730 water molecules, 2 bound glutamate molecules, and 2 Tris molecules from the buffer used in crystallization. The final R(cryst) and R(free) factors are 13.61% and 16.89%, respectively.

Protein Classification

Transport protein

Structure Weight

64851.95 Da

Polymer

1

Molecule

Periplasmic Binding Transport Protein

Chain Length

287 amino acids

PDB ID

2VHA

MMDB ID

70491

Source

E.coli

Method

X-Ray Diffraction

Resolution

2.8Å

Ligand Chemical Component

Glutamic acid; 2-amino-2-hydroxymethyl-propane-1,3-diol

Gene Name

livJ

Synonyms

S4285

Gene ID

1080493

Function

Transport activity

Reference

Hu, Y.L., Fan, C.-P., Fu, G.S., Zhu, D.Y., Jin, Q., Wang, D.-C. (2008) Crystal Structure of a Glutamate/Aspartate Binding Protein Complexed with a Glutamate Molecule: Structural Basis of Ligand Specificity at Atomic Resolution. J.Mol.Biol. 382: 99-111