1te6

Crystal Structure of Human Neuron Specific Enolase at 1.8 angstrom

spinqualitylabelsall models 1te6, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1te6 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, MG, PO4, TRS Gene: ENO2 (Homo sapiens) Activity: Phosphopyruvate hydratase, with EC number 4.2.1.11 Resources: FirstGlance, OCA, RCSB, PDBsum Function [ENOG_HUMAN] Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Enolase

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