1te6
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1te6 |SIZE=350|CAPTION= <scene name='initialview01'>1te6</scene>, resolution 1.80Å | |PDB= 1te6 |SIZE=350|CAPTION= <scene name='initialview01'>1te6</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </span> |
|GENE= ENO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= ENO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1te6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1te6 OCA], [http://www.ebi.ac.uk/pdbsum/1te6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1te6 RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Lovelace, L.]] | [[Category: Lovelace, L.]] | ||
[[Category: Minor, W.]] | [[Category: Minor, W.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: PO4]] | ||
| - | [[Category: TRS]] | ||
[[Category: enolase]] | [[Category: enolase]] | ||
[[Category: isozyme]] | [[Category: isozyme]] | ||
| Line 39: | Line 38: | ||
[[Category: surface charge]] | [[Category: surface charge]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:54:49 2008'' |
Revision as of 20:54, 30 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | ENO2 (Homo sapiens) | ||||||
| Activity: | Phosphopyruvate hydratase, with EC number 4.2.1.11 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 30 23:54:49 2008
