DEBP, Periplasmic Binding Transport Protein

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DEBP Protein Crystal(CBCRY22)

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Product Summary
Name	DEBP Protein Crystal Download Datasheet

Background
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.

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.

Molecular Description
Protein Classification	Transport protein
Structure Weight	64851.95 Da
Polymer	1
Molecule	Periplasmic Binding Transport Protein
Chain Length	287 amino acids

Crystal Description
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 Information
Gene Name	livJ
Synonyms	S4285
Gene ID	1080493
Function	Transport activity

Reference
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

DEBP Protein Crystal

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DEBP Protein Crystal(CBCRY22)

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