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1h1c

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(New page: 200px<br /> <applet load="1h1c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h1c, resolution 2.85&Aring;" /> '''HISTIDINOL-PHOSPHAT...)
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[[Image:1h1c.gif|left|200px]]<br />
 
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<applet load="1h1c" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1h1c, resolution 2.85&Aring;" />
 
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'''HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA'''<br />
 
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==Overview==
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==Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima==
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In histidine biosynthesis, histidinol-phosphate aminotransferase catalyzes, the transfer of the amino group from glutamate to imidazole, acetol-phosphate producing 2-oxoglutarate and histidinol phosphate. In, some organisms such as the hyperthermophile Thermotoga maritima, specific, tyrosine and aromatic amino acid transaminases have not been identified to, date, suggesting an additional role for histidinol-phosphate, aminotransferase in other transamination reactions generating aromatic, amino acids. To gain insight into the specific function of this, transaminase, we have determined its crystal structure in the absence of, any ligand except phosphate, in the presence of covalently bound pyridoxal, 5'-phosphate, of the coenzyme histidinol phosphate adduct, and of, pyridoxamine ... [[http://ispc.weizmann.ac.il/pmbin/getpm?15007066 (full description)]]
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<StructureSection load='1h1c' size='340' side='right'caption='[[1h1c]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1h1c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H1C 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]] 2.85&#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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=1h1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h1c OCA], [https://pdbe.org/1h1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h1c RCSB], [https://www.ebi.ac.uk/pdbsum/1h1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h1c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HIS8_THEMA HIS8_THEMA]
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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/h1/1h1c_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=1h1c ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1H1C is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]] with PLP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H1C OCA]].
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*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase., Fernandez FJ, Vega MC, Lehmann F, Sandmeier E, Gehring H, Christen P, Wilmanns M, J Biol Chem. 2004 May 14;279(20):21478-88. Epub 2004 Mar 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15007066 15007066]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Fernandez, F.J.]]
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[[Category: Fernandez FJ]]
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[[Category: Vega, M.C.]]
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[[Category: Vega MC]]
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[[Category: Wilmanns, M.]]
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[[Category: Wilmanns M]]
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[[Category: PLP]]
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[[Category: aminotransferase]]
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[[Category: histidine biosynthesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:23:19 2007''
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Current revision

Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima

PDB ID 1h1c

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