7xmv

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Current revision (07:27, 3 July 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7xmv]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MG1655 Escherichia coli str. K-12 substr. MG1655]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XMV FirstGlance]. <br>
<table><tr><td colspan='2'>[[7xmv]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MG1655 Escherichia coli str. K-12 substr. MG1655]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XMV FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=HSX:5-O-PHOSPHONO-ALPHA-D-RIBOFURANOSE'>HSX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=HSX:5-O-PHOSPHONO-ALPHA-D-RIBOFURANOSE'>HSX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7xmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xmv OCA], [https://pdbe.org/7xmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xmv RCSB], [https://www.ebi.ac.uk/pdbsum/7xmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xmv ProSAT]</span></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=7xmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xmv OCA], [https://pdbe.org/7xmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xmv RCSB], [https://www.ebi.ac.uk/pdbsum/7xmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xmv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/KPRS_ECOLI KPRS_ECOLI]] Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).[HAMAP-Rule:MF_00583]<ref>PMID:10954724</ref> <ref>PMID:2542328</ref> <ref>PMID:3009477</ref> <ref>PMID:6290219</ref> <ref>PMID:7657655</ref> <ref>PMID:8679571</ref> <ref>PMID:9125530</ref>
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[https://www.uniprot.org/uniprot/KPRS_ECOLI KPRS_ECOLI] Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).[HAMAP-Rule:MF_00583]<ref>PMID:10954724</ref> <ref>PMID:2542328</ref> <ref>PMID:3009477</ref> <ref>PMID:6290219</ref> <ref>PMID:7657655</ref> <ref>PMID:8679571</ref> <ref>PMID:9125530</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Phosphoribosyl pyrophosphate (PRPP) is a key intermediate in the biosynthesis of purine and pyrimidine nucleotides, histidine, tryptophan, and cofactors NAD and NADP. Abnormal regulation of PRPP synthase (PRPS) is associated with human disorders, including Arts syndrome, retinal dystrophy, and gouty arthritis. Recent studies have demonstrated that PRPS can form filamentous cytoophidia in eukaryotes. Here, we show that PRPS forms cytoophidia in prokaryotes both in vitro and in vivo. Moreover, we solve two distinct filament structures of E. coli PRPS at near-atomic resolution using Cryo-EM. The formation of the two types of filaments is controlled by the binding of different ligands. One filament type is resistant to allosteric inhibition. The structural comparison reveals conformational changes of a regulatory flexible loop, which may regulate the binding of the allosteric inhibitor and the substrate ATP. A noncanonical allosteric AMP/ADP binding site is identified to stabilize the conformation of the regulatory flexible loop. Our findings not only explore a new mechanism of PRPS regulation with structural basis, but also propose an additional layer of cell metabolism through PRPS filamentation.
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Filamentation modulates allosteric regulation of PRPS.,Hu HH, Lu GM, Chang CC, Li Y, Zhong J, Guo CJ, Zhou X, Yin B, Zhang T, Liu JL Elife. 2022 Jun 23;11:e79552. doi: 10.7554/eLife.79552. PMID:35736577<ref>PMID:35736577</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7xmv" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Current revision

E.coli phosphoribosylpyrophosphate (PRPP) synthetase type A(AMP/ADP) filament bound with ADP, AMP and R5P

PDB ID 7xmv

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