7z6r: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[7z6r]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Psychrobacter_arcticus Psychrobacter arcticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z6R FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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]] 2.55&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=PRP:ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC+ACID'>PRP</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=7z6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z6r OCA], [https://pdbe.org/7z6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z6r RCSB], [https://www.ebi.ac.uk/pdbsum/7z6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z6r ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/HISZ_PSYA2 HISZ_PSYA2] Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.[HAMAP-Rule:MF_00125]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-ATP phosphoribosyltransferase catalyses the first step of histidine biosynthesis and is controlled via a complex allosteric mechanism where the regulatory protein HisZ enhances catalysis by the catalytic protein HisG(S) while mediating allosteric inhibition by histidine. Activation by HisZ was proposed to position HisG(S) Arg56 to stabilise departure of the pyrophosphate leaving group. Here we report active-site mutants of HisG(S) with impaired reaction chemistry which can be allosterically restored by HisZ despite the HisZ:HisG(S) interface lying ~20 A away from the active site. MD simulations indicate HisZ binding constrains the dynamics of HisG(S) to favour a preorganised active site where both Arg56 and Arg32 are poised to stabilise leaving-group departure in WT-HisG(S). In the Arg56Ala-HisG(S) mutant, HisZ modulates Arg32 dynamics so that it can partially compensate for the absence of Arg56. These results illustrate how remote protein-protein interactions translate into catalytic resilience by restoring damaged electrostatic preorganisation at the active site.
-Allosteric rescue of catalytically impaired ATP phosphoribosyltransferase variants links protein dynamics to active-site electrostatic preorganisation.,Fisher G, Corbella M, Alphey MS, Nicholson J, Read BJ, Kamerlin SCL, da Silva RG Nat Commun. 2022 Dec 9;13(1):7607. doi: 10.1038/s41467-022-34960-9. PMID:36494361<ref>PMID:36494361</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 7z6r" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[ATP phosphoribosyl transferase 3D structures|ATP phosphoribosyl transferase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>