1usy: Difference between revisions

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-[[Image:1usy.png|left|200px]]
-<!--
+==ATP phosphoribosyl transferase (HisG:HisZ) complex from Thermotoga maritima==
-The line below this paragraph, containing "STRUCTURE_1usy", creates the "Structure Box" on the page.
+<StructureSection load='1usy' size='340' side='right'caption='[[1usy]], [[Resolution|resolution]] 2.52&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'>[[1usy]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1USY 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]] 2.52&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-{{STRUCTURE_1usy|  PDB=1usy  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1usy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1usy OCA], [https://pdbe.org/1usy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1usy RCSB], [https://www.ebi.ac.uk/pdbsum/1usy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1usy ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HISZ_THEMA HISZ_THEMA] Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity).
+== 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/us/1usy_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1usy ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The molecular structure of the ATP phosphoribosyl transferase from the hyperthermophile Thermotoga maritima is composed of a 220 kDa hetero-octameric complex comprising four catalytic subunits (HisGS) and four regulatory subunits (HisZ). Steady-state kinetics indicate that only the complete octameric complex is active and non-competitively inhibited by the pathway product histidine. The rationale for these findings is provided by the crystal structure revealing a total of eight histidine binding sites that are located within each of the four HisGS-HisZ subunit interfaces formed by the ATP phosphoribosyl transferase complex. While the structure of the catalytic HisGS subunit is related to the catalytic domain of another family of (HisGL)2 ATP phosphoribosyl transferases that is functional in the absence of additional regulatory subunits, the structure of the regulatory HisZ subunit is distantly related to class II aminoacyl-tRNA synthetases. However, neither the mode of the oligomeric subunit arrangement nor the type of histidine binding pockets is found in these structural relatives. Common ancestry of the regulatory HisZ subunit and class II aminoacyl-tRNA synthetase may reflect the balanced need of regulated amounts of a cognate amino acid (histidine) in the translation apparatus, ultimately linking amino acid biosynthesis and protein biosynthesis in terms of function, structure and evolution.
-===ATP PHOSPHORIBOSYL TRANSFERASE (HISG:HISZ) COMPLEX FROM THERMOTOGA MARITIMA===
+Regulation of the hetero-octameric ATP phosphoribosyl transferase complex from Thermotoga maritima by a tRNA synthetase-like subunit.,Vega MC, Zou P, Fernandez FJ, Murphy GE, Sterner R, Popov A, Wilmanns M Mol Microbiol. 2005 Feb;55(3):675-86. PMID:15660995<ref>PMID:15660995</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_15660995}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1usy" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 15660995 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_15660995}}
-==About this Structure==
-[[1usy]] is a 8 chain structure of [[ATP Phosphoribosyl Transferase]] 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=1USY OCA].
 ==See Also==
-*[[ATP Phosphoribosyl Transferase]]
+*[[ATP phosphoribosyl transferase 3D structures|ATP phosphoribosyl transferase 3D structures]]
-*[[User:Lawrence Sheringham Borketey/ATP Phosphoribosyl Transferase (HisG)]]
+== References ==
+<references/>
-==Reference==
+__TOC__
-<ref group="xtra">PMID:015660995</ref><references group="xtra"/>
+</StructureSection>
-[[Category: ATP phosphoribosyltransferase]]
+[[Category: Large Structures]]
-[[Category: Thermotoga maritima]]
+[[Category: Thermotoga maritima MSB8]]
-[[Category: Fernandez, F J.]]
+[[Category: Fernandez FJ]]
-[[Category: Murphy, G E.]]
+[[Category: Murphy GE]]
-[[Category: Popov, A.]]
+[[Category: Popov A]]
-[[Category: Vega, M C.]]
+[[Category: Vega MC]]
-[[Category: Wilmanns, M.]]
+[[Category: Wilmanns M]]
-[[Category: Zou, P.]]
+[[Category: Zou P]]
-[[Category: Aminoacyl-trna synthetase]]
-[[Category: Atp phosphoribosyl transferase]]
-[[Category: Transferase]]