1te6
From Proteopedia
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Crystal Structure of Human Neuron Specific Enolase at 1.8 angstrom
Overview
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.
About this Structure
1TE6 is a Single protein structure of sequence from Homo sapiens with , , and as ligands. Active as Phosphopyruvate hydratase, with EC number 4.2.1.11 Full crystallographic information is available from OCA.
Reference
Expression, purification and the 1.8 angstroms resolution crystal structure of human neuron specific enolase., Chai G, Brewer JM, Lovelace LL, Aoki T, Minor W, Lebioda L, J Mol Biol. 2004 Aug 20;341(4):1015-21. PMID:15289101
Page seeded by OCA on Thu Feb 21 15:12:36 2008
Categories: Homo sapiens | Phosphopyruvate hydratase | Single protein | Aoki, T. | Brewer, J. | Chai, G. | Lebioda, L. | Lovelace, L. | Minor, W. | CL | MG | PO4 | TRS | Enolase | Isozymes | Negative cooperativity | Neurons | Surface charges
