1TE6

Crystal Structure of Human Neuron Specific Enolase at 1.8 angstrom

Summary for 1TE6

• Entry DOI: 10.2210/pdb1te6/pdb
• Descriptor: Gamma enolase, MAGNESIUM ION, PHOSPHATE ION, ... (6 entities in total)
• Functional Keywords: enolase, neurons, isozymes, surface charges, negative cooperativity, lyase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm (By similarity): P09104
• Total number of polymer chains: 2
• Total formula weight: 96361.64

Authors

Chai, G.,Brewer, J.,Lovelace, L.,Aoki, T.,Minor, W.,Lebioda, L. (deposition date: 2004-05-24, release date: 2004-09-21, Last modification date: 2023-08-23)

Primary citation

Chai, G.,Brewer, J.,Lovelace, L.,Aoki, T.,Minor, W.,Lebioda, L.
Expression, Purification and the 1.8 A Resolution Crystal Structure of Human Neuron Specific Enolase
J.Mol.Biol., 341:1015-1021, 2004

PubMed Abstract: Human neuron-specific enolase (NSE) or isozyme gamma has been expressed with a C-terminal His-tag in Escherichia coli. The enzyme has been purified, crystallized and its crystal structure determined. In the crystals the enzyme forms the asymmetric complex NSE x Mg2 x SO4/NSE x Mg x Cl, where "/" separates the dimer subunits. The subunit that contains the sulfate (or phosphate) ion and two magnesium ions is in the closed conformation observed in enolase complexes with the substrate or its analogues; the other subunit is in the open conformation observed in enolase subunits without bound substrate or analogues. This indicates negative cooperativity for ligand binding between subunits. Electrostatic charge differences between isozymes alpha and gamma, -19 at physiological pH, are concentrated in the regions of the molecular surface that are negatively charged in alpha, i.e. surface areas negatively charged in alpha are more negatively charged in gamma, while areas that are neutral or positively charged tend to be charge-conserved.

PubMed: 15289101
DOI: 10.1016/j.jmb.2004.05.068

Experimental method

X-RAY DIFFRACTION (1.8 Å)