4s2u: Difference between revisions

Revision as of 10:41, 15 March 2023

Crystal structure of the Phosphorybosylpyrophosphate synthetase from E. Coli

Structural highlights

4s2u is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	MG
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

References

↑ Willemoes M, Hove-Jensen B, Larsen S. Steady state kinetic model for the binding of substrates and allosteric effectors to Escherichia coli phosphoribosyl-diphosphate synthase. J Biol Chem. 2000 Nov 10;275(45):35408-12. doi: 10.1074/jbc.M006346200. PMID:10954724 doi:https://dx.doi.org/10.1074/jbc.M006346200
↑ Bower SG, Harlow KW, Switzer RL, Hove-Jensen B. Characterization of the Escherichia coli prsA1-encoded mutant phosphoribosylpyrophosphate synthetase identifies a divalent cation-nucleotide binding site. J Biol Chem. 1989 Jun 15;264(17):10287-91. PMID:2542328
↑ Hove-Jensen B, Harlow KW, King CJ, Switzer RL. Phosphoribosylpyrophosphate synthetase of Escherichia coli. Properties of the purified enzyme and primary structure of the prs gene. J Biol Chem. 1986 May 25;261(15):6765-71. PMID:3009477
↑ Hove-Jensen B, Nygaard P. Phosphoribosylpyrophosphate synthetase of Escherichia coli, Identification of a mutant enzyme. Eur J Biochem. 1982 Aug;126(2):327-32. doi: 10.1111/j.1432-1033.1982.tb06782.x. PMID:6290219 doi:https://dx.doi.org/10.1111/j.1432-1033.1982.tb06782.x
↑ Hilden I, Hove-Jensen B, Harlow KW. Inactivation of Escherichia coli phosphoribosylpyrophosphate synthetase by the 2',3'-dialdehyde derivative of ATP. Identification of active site lysines. J Biol Chem. 1995 Sep 1;270(35):20730-6. doi: 10.1074/jbc.270.35.20730. PMID:7657655 doi:https://dx.doi.org/10.1074/jbc.270.35.20730
↑ Willemoes M, Nilsson D, Hove-Jensen B. Effects of mutagenesis of aspartic acid residues in the putative phosphoribosyl diphosphate binding site of Escherichia coli phosphoribosyl diphosphate synthetase on metal ion specificity and ribose 5-phosphate binding. Biochemistry. 1996 Jun 25;35(25):8181-6. doi: 10.1021/bi9528560. PMID:8679571 doi:https://dx.doi.org/10.1021/bi9528560
↑ Willemoes M, Hove-Jensen B. Binding of divalent magnesium by Escherichia coli phosphoribosyl diphosphate synthetase. Biochemistry. 1997 Apr 22;36(16):5078-83. doi: 10.1021/bi962610a. PMID:9125530 doi:https://dx.doi.org/10.1021/bi962610a

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OCA

[1] Willemoes M, Hove-Jensen B, Larsen S. Steady state kinetic model for the binding of substrates and allosteric effectors to Escherichia coli phosphoribosyl-diphosphate synthase. J Biol Chem. 2000 Nov 10;275(45):35408-12. doi: 10.1074/jbc.M006346200. PMID:10954724 doi:https://dx.doi.org/10.1074/jbc.M006346200

[2] Bower SG, Harlow KW, Switzer RL, Hove-Jensen B. Characterization of the Escherichia coli prsA1-encoded mutant phosphoribosylpyrophosphate synthetase identifies a divalent cation-nucleotide binding site. J Biol Chem. 1989 Jun 15;264(17):10287-91. PMID:2542328

[3] Hove-Jensen B, Harlow KW, King CJ, Switzer RL. Phosphoribosylpyrophosphate synthetase of Escherichia coli. Properties of the purified enzyme and primary structure of the prs gene. J Biol Chem. 1986 May 25;261(15):6765-71. PMID:3009477

[4] Hove-Jensen B, Nygaard P. Phosphoribosylpyrophosphate synthetase of Escherichia coli, Identification of a mutant enzyme. Eur J Biochem. 1982 Aug;126(2):327-32. doi: 10.1111/j.1432-1033.1982.tb06782.x. PMID:6290219 doi:https://dx.doi.org/10.1111/j.1432-1033.1982.tb06782.x

[5] Hilden I, Hove-Jensen B, Harlow KW. Inactivation of Escherichia coli phosphoribosylpyrophosphate synthetase by the 2',3'-dialdehyde derivative of ATP. Identification of active site lysines. J Biol Chem. 1995 Sep 1;270(35):20730-6. doi: 10.1074/jbc.270.35.20730. PMID:7657655 doi:https://dx.doi.org/10.1074/jbc.270.35.20730

[6] Willemoes M, Nilsson D, Hove-Jensen B. Effects of mutagenesis of aspartic acid residues in the putative phosphoribosyl diphosphate binding site of Escherichia coli phosphoribosyl diphosphate synthetase on metal ion specificity and ribose 5-phosphate binding. Biochemistry. 1996 Jun 25;35(25):8181-6. doi: 10.1021/bi9528560. PMID:8679571 doi:https://dx.doi.org/10.1021/bi9528560

[7] Willemoes M, Hove-Jensen B. Binding of divalent magnesium by Escherichia coli phosphoribosyl diphosphate synthetase. Biochemistry. 1997 Apr 22;36(16):5078-83. doi: 10.1021/bi962610a. PMID:9125530 doi:https://dx.doi.org/10.1021/bi962610a

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[4]

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@@ Line 3: / Line 3: @@
 <StructureSection load='4s2u' size='340' side='right'caption='[[4s2u]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4s2u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4S2U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4s2u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4S2U FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">prsA, prs ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=4s2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2u OCA], [https://pdbe.org/4s2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4s2u RCSB], [https://www.ebi.ac.uk/pdbsum/4s2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4s2u 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/Ribose-phosphate_diphosphokinase Ribose-phosphate diphosphokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.6.1 2.7.6.1] </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=4s2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2u OCA], [http://pdbe.org/4s2u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4s2u RCSB], [http://www.ebi.ac.uk/pdbsum/4s2u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4s2u ProSAT]</span></td></tr>
 </table>
+== Function ==
+[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>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Ribose-phosphate diphosphokinase]]
+[[Category: Abramchik YA]]
-[[Category: Abramchik, Y A]]
+[[Category: Esipov RS]]
-[[Category: Esipov, R S]]
+[[Category: Iaroslavtceva AK]]
-[[Category: Iaroslavtceva, A K]]
+[[Category: Kuranova IP]]
-[[Category: Kuranova, I P]]
+[[Category: Muravieva TI]]
-[[Category: Muravieva, T I]]
+[[Category: Stepanenko VN]]
-[[Category: Stepanenko, V N]]
+[[Category: Timofeev VI]]
-[[Category: Timofeev, V I]]
+[[Category: Zhukhlistova NE]]
-[[Category: Zhukhlistova, N E]]
-[[Category: Atp binding]]
-[[Category: Synthetase]]
-[[Category: Transferase]]

4s2u: Difference between revisions

Revision as of 10:41, 15 March 2023

Crystal structure of the Phosphorybosylpyrophosphate synthetase from E. Coli

Structural highlights

Function

References

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