1z7n: Difference between revisions

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 ==ATP Phosphoribosyl transferase (HisZG ATP-PRTase) from Lactococcus lactis with bound PRPP substrate==
-<StructureSection load='1z7n' size='340' side='right' caption='[[1z7n]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
+<StructureSection load='1z7n' size='340' side='right'caption='[[1z7n]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1z7n]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z7N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1z7n]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z7N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z7N FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PRP:ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC+ACID'>PRP</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.25&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z7m|1z7m]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PRP:ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC+ACID'>PRP</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hisZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 "Bacterium lactis" Lister 1873]), hisG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 "Bacterium lactis" Lister 1873])</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=1z7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z7n OCA], [https://pdbe.org/1z7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z7n RCSB], [https://www.ebi.ac.uk/pdbsum/1z7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z7n ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ATP_phosphoribosyltransferase ATP phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.17 2.4.2.17] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z7n OCA], [http://pdbe.org/1z7n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z7n RCSB], [http://www.ebi.ac.uk/pdbsum/1z7n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z7n ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HISZ_LACLA HISZ_LACLA]] Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.[HAMAP-Rule:MF_00125] [[http://www.uniprot.org/uniprot/HIS1_LACLA HIS1_LACLA]] Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.[HAMAP-Rule:MF_01018]
+[https://www.uniprot.org/uniprot/HISZ_LACLA HISZ_LACLA] Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.[HAMAP-Rule:MF_00125]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 22: / Line 20: @@
 </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=1z7n ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-ATP phosphoribosyl transferase (ATP-PRT) joins ATP and 5-phosphoribosyl-1-pyrophosphate (PRPP) in a highly regulated reaction that initiates histidine biosynthesis. The unusual hetero-octameric version of ATP-PRT includes four HisG(S) catalytic subunits based on the periplasmic binding protein fold and four HisZ regulatory subunits that resemble histidyl-tRNA synthetases. Here, we present the first structure of a PRPP-bound ATP-PRT at 2.9 A and provide a structural model for allosteric activation based on comparisons with other inhibited and activated ATP-PRTs from both the hetero-octameric and hexameric families. The activated state of the octameric enzyme is characterized by an interstitial phosphate ion in the HisZ-HisG interface and new contacts between the HisZ motif 2 loop and the HisG(S) dimer interface. These contacts restructure the interface to recruit conserved residues to the active site, where they activate pyrophosphate to promote catalysis. Additionally, mutational analysis identifies the histidine binding sites within a region highly conserved between HisZ and the functional HisRS. Through the oligomerization and functional re-assignment of protein domains associated with aminoacylation and phosphate binding, the HisZ-HisG octameric ATP-PRT acquired the ability to initiate the synthesis of a key metabolic intermediate in an allosterically regulated fashion.
-Activation of the hetero-octameric ATP phosphoribosyl transferase through subunit interface rearrangement by a tRNA synthetase paralog.,Champagne KS, Sissler M, Larrabee Y, Doublie S, Francklyn CS J Biol Chem. 2005 Oct 7;280(40):34096-104. Epub 2005 Jul 28. PMID:16051603<ref>PMID:16051603</ref>
+==See Also==
+*[[ATP Phosphoribosyl Transferase|ATP Phosphoribosyl Transferase]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+*[[ATP phosphoribosyl transferase 3D structures|ATP phosphoribosyl transferase 3D structures]]
-</div>
-<div class="pdbe-citations 1z7n" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacterium lactis lister 1873]]
+[[Category: Lactococcus lactis]]
-[[Category: ATP phosphoribosyltransferase]]
+[[Category: Large Structures]]
-[[Category: Champagne, K S]]
+[[Category: Champagne KS]]
-[[Category: Doublie, S]]
+[[Category: Doublie S]]
-[[Category: Francklyn, C S]]
+[[Category: Francklyn CS]]
-[[Category: Larrabee, Y]]
+[[Category: Larrabee Y]]
-[[Category: Sissler, M]]
+[[Category: Sissler M]]
-[[Category: Allosteric]]
-[[Category: Atp-prt]]
-[[Category: Histidine biosynthesis]]
-[[Category: Hiszg]]
-[[Category: Prpp]]
-[[Category: Transferase]]