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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[[Image:1te6.gif|left|200px]]<br />
 
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<applet load="1te6" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1te6, resolution 1.80&Aring;" />
 
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'''Crystal Structure of Human Neuron Specific Enolase at 1.8 angstrom'''<br />
 
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==Overview==
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==Crystal Structure of Human Neuron Specific Enolase at 1.8 angstrom==
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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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<StructureSection load='1te6' size='340' side='right'caption='[[1te6]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1te6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TE6 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1te6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1te6 OCA], [https://pdbe.org/1te6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1te6 RCSB], [https://www.ebi.ac.uk/pdbsum/1te6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1te6 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ENOG_HUMAN 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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/te/1te6_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1te6 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==About this Structure==
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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<ref>PMID:15289101</ref>
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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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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15289101 15289101]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 1te6" style="background-color:#fffaf0;"></div>
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[[Category: Phosphopyruvate hydratase]]
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[[Category: Single protein]]
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[[Category: Aoki, T.]]
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[[Category: Brewer, J.]]
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[[Category: Chai, G.]]
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[[Category: Lebioda, L.]]
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[[Category: Lovelace, L.]]
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[[Category: Minor, W.]]
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[[Category: CL]]
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[[Category: MG]]
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[[Category: PO4]]
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[[Category: TRS]]
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[[Category: enolase]]
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[[Category: isozymes]]
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[[Category: negative cooperativity]]
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[[Category: neurons]]
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[[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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==See Also==
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*[[Enolase 3D structures|Enolase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Aoki T]]
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[[Category: Brewer J]]
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[[Category: Chai G]]
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[[Category: Lebioda L]]
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[[Category: Lovelace L]]
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[[Category: Minor W]]

Current revision

Crystal Structure of Human Neuron Specific Enolase at 1.8 angstrom

PDB ID 1te6

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