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| | ==Adenosine triphosphate phosphoribosyltransferase from Campylobacter jejuni in complex with ATP== | | ==Adenosine triphosphate phosphoribosyltransferase from Campylobacter jejuni in complex with ATP== |
| - | <StructureSection load='4yb7' size='340' side='right' caption='[[4yb7]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='4yb7' size='340' side='right'caption='[[4yb7]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4yb7]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Camjr Camjr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YB7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YB7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4yb7]] is a 12 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=4YB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YB7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yb5|4yb5]], [[4yb6|4yb6]]</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=4yb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yb7 OCA], [https://pdbe.org/4yb7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yb7 RCSB], [https://www.ebi.ac.uk/pdbsum/4yb7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yb7 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hisG, CJE1769 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=195099 CAMJR])</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>
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| - | <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=4yb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yb7 OCA], [http://pdbe.org/4yb7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yb7 RCSB], [http://www.ebi.ac.uk/pdbsum/4yb7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yb7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4yb7" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4yb7" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[ATP phosphoribosyl transferase 3D structures|ATP phosphoribosyl transferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: ATP phosphoribosyltransferase]] | + | [[Category: Campylobacter jejuni RM1221]] |
| - | [[Category: Camjr]] | + | [[Category: Large Structures]] |
| - | [[Category: Mittelstaedt, G]] | + | [[Category: Mittelstaedt G]] |
| - | [[Category: Moggre, G J]] | + | [[Category: Moggre G-J]] |
| - | [[Category: Parker, E J]] | + | [[Category: Parker EJ]] |
| - | [[Category: Atp]]
| + | |
| - | [[Category: Hexamer]]
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| - | [[Category: Phosphoribosyltransferase]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
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.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mittelstadt G, Moggre GJ, Panjikar S, Nazmi AR, Parker EJ. Campylobacter jejuni adenosine triphosphate phosphoribosyltransferase is an active hexamer that is allosterically controlled by the twisting of a regulatory tail. Protein Sci. 2016 Aug;25(8):1492-506. doi: 10.1002/pro.2948. Epub 2016 Jun 6. PMID:27191057 doi:http://dx.doi.org/10.1002/pro.2948
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