1uu1: Difference between revisions

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-[[Image:1uu1.png|left|200px]]
-<!--
+==Complex of Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima (Apo-form)==
-The line below this paragraph, containing "STRUCTURE_1uu1", creates the "Structure Box" on the page.
+<StructureSection load='1uu1' size='340' side='right'caption='[[1uu1]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1uu1]] 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=1UU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UU1 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HSA:PHOSPHORIC+ACID+MONO-[2-AMINO-3-(3H-IMIDAZOL-4-YL)-PROPYL]ESTER'>HSA</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene></td></tr>
-{{STRUCTURE_1uu1|  PDB=1uu1  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uu1 OCA], [https://pdbe.org/1uu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uu1 RCSB], [https://www.ebi.ac.uk/pdbsum/1uu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uu1 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/uu/1uu1_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=1uu1 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===COMPLEX OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA (APO-FORM)===
+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:15007066<ref>PMID:15007066</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_15007066}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1uu1" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 15007066 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_15007066}}
-==About this Structure==
-[[1uu1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UU1 OCA].
 ==See Also==
-*[[User:Eric Martz]]
+*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:15007066</ref><ref group="xtra">PMID:11518529</ref><references group="xtra"/>
+__TOC__
-[[Category: Histidinol-phosphate transaminase]]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Thermotoga maritima]]
-[[Category: Fernandez, F J.]]
+[[Category: Fernandez FJ]]
-[[Category: Lehman, F.]]
+[[Category: Lehman F]]
-[[Category: Vega, M C.]]
+[[Category: Vega MC]]
-[[Category: Wilmanns, M.]]
+[[Category: Wilmanns M]]
-[[Category: Aminotransferase]]
-[[Category: Complete proteome]]
-[[Category: Histidine biosynthesis]]
-[[Category: Pyridoxal phosphate]]
-[[Category: Transferase]]