4yb5
From Proteopedia
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==Adenosine triphosphate phosphoribosyltransferase from Campylobacter jejuni in complex with the allosteric inhibitor histidine== | ==Adenosine triphosphate phosphoribosyltransferase from Campylobacter jejuni in complex with the allosteric inhibitor histidine== | ||
| - | <StructureSection load='4yb5' size='340' side='right' caption='[[4yb5]], [[Resolution|resolution]] 2.24Å' scene=''> | + | <StructureSection load='4yb5' size='340' side='right'caption='[[4yb5]], [[Resolution|resolution]] 2.24Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4yb5]] is a 6 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4yb5]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni_RM1221 Campylobacter jejuni RM1221]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YB5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.24Å</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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</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=4yb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yb5 OCA], [https://pdbe.org/4yb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yb5 RCSB], [https://www.ebi.ac.uk/pdbsum/4yb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yb5 ProSAT]</span></td></tr> | |
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/HIS1_CAMJR HIS1_CAMJR] 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. |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Adenosine triphosphate phosphoribosyltransferase (ATP-PRT) catalyzes the first committed step of the histidine biosynthesis in plants and microorganisms. Here, we present the functional and structural characterization of the ATP-PRT from the pathogenic epsilon-proteobacteria Campylobacter jejuni (CjeATP-PRT). This enzyme is a member of the long form (HisGL ) ATP-PRT and is allosterically inhibited by histidine, which binds to a remote regulatory domain, and competitively inhibited by AMP. In the crystalline form, CjeATP-PRT was found to adopt two distinctly different hexameric conformations, with an open homohexameric structure observed in the presence of substrate ATP, and a more compact closed form present when inhibitor histidine is bound. CjeATP-PRT was observed to adopt only a hexameric quaternary structure in solution, contradicting previous hypotheses favoring an allosteric mechanism driven by an oligomer equilibrium. Instead, this study supports the conclusion that the ATP-PRT long form hexamer is the active species; the tightening of this structure in response to remote histidine binding results in an inhibited enzyme. | ||
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| + | Campylobacter jejuni adenosine triphosphate phosphoribosyltransferase is an active hexamer that is allosterically controlled by the twisting of a regulatory tail.,Mittelstadt G, Moggre GJ, Panjikar S, Nazmi AR, Parker EJ Protein Sci. 2016 Aug;25(8):1492-506. doi: 10.1002/pro.2948. Epub 2016 Jun 6. PMID:27191057<ref>PMID:27191057</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4yb5" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[ATP phosphoribosyl transferase 3D structures|ATP phosphoribosyl transferase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Campylobacter jejuni RM1221]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Mittelstaedt | + | [[Category: Mittelstaedt G]] |
| - | [[Category: Moggre | + | [[Category: Moggre G-J]] |
| - | [[Category: Parker | + | [[Category: Parker EJ]] |
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Current revision
Adenosine triphosphate phosphoribosyltransferase from Campylobacter jejuni in complex with the allosteric inhibitor histidine
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