1h1c: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1h1c.gif|left|200px]]<br /><applet load="1h1c" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1h1c, resolution 2.85&Aring;" />
-'''HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA'''<br />
-==Overview==
+==Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima==
-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 5'-phosphate. The enzyme accepts histidinol phosphate, tyrosine, tryptophan, and phenylalanine, but not histidine, as substrates., The structures provide a model of how these different substrates could be, accommodated by histidinol-phosphate aminotransferase. Some of the, structural features of the enzyme are more preserved between the T., maritima enzyme and a related threonine-phosphate decarboxylase from S., typhimurium than with histidinol-phosphate aminotransferases from, different organisms.
+<StructureSection load='1h1c' size='340' side='right'caption='[[1h1c]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+<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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HIS8_THEMA HIS8_THEMA]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h1/1h1c_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-H1C 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 <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Histidinol-phosphate_transaminase Histidinol-phosphate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9] Known structural/functional Site: <scene name='pdbsite=AC1:Plp+Binding+Site+For+Chain+D'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1C OCA].
+*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-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]
+[[Category: Large Structures]]
-[[Category: Histidinol-phosphate transaminase]]
-[[Category: Single protein]]
 [[Category: Thermotoga maritima]]
-[[Category: Fernandez, F.J.]]
+[[Category: Fernandez FJ]]
-[[Category: Vega, M.C.]]
+[[Category: Vega MC]]
-[[Category: Wilmanns, M.]]
+[[Category: Wilmanns M]]
-[[Category: PLP]]
-[[Category: aminotransferase]]
-[[Category: histidine biosynthesis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:45:06 2008''