1te6

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(New page: 200px<br /> <applet load="1te6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1te6, resolution 1.80&Aring;" /> '''Crystal Structure o...)
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'''Crystal Structure of Human Neuron Specific Enolase at 1.8 angstrom'''<br />
'''Crystal Structure of Human Neuron Specific Enolase at 1.8 angstrom'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1TE6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG, PO4, CL and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TE6 OCA].
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1TE6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TE6 OCA].
==Reference==
==Reference==
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[[Category: surface charges]]
[[Category: surface charges]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:23:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:36 2008''

Revision as of 13:12, 21 February 2008


1te6, resolution 1.80Å

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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

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