4s2u: Difference between revisions

Latest revision as of 12:57, 1 March 2024

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.
Method:	X-ray diffraction, Resolution 2.71Å
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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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4s2u is ON HOLD
+==Crystal structure of the Phosphorybosylpyrophosphate synthetase from E. Coli==
+<StructureSection load='4s2u' size='340' side='right'caption='[[4s2u]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
-Authors: Timofeev, V.I., Abramchik, Yu.A., Muravieva, T.I., Iaroslavtceva, A.K., Stepanenko, V.N., Zhukhlistova, N.E., Esipov, R.S., Kuranova, I.P.
+== Structural highlights ==
+<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>
-Description: Crystal structure of the Phosphorybosylpyrophosphate synthetase from E. Coli
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.71&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<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>
-[[Category: Kuranova, I.P]]
+<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>
-[[Category: Stepanenko, V.N]]
+</table>
-[[Category: Iaroslavtceva, A.K]]
+== Function ==
-[[Category: Abramchik, Yu.A]]
+[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>
-[[Category: Esipov, R.S]]
+== References ==
-[[Category: Timofeev, V.I]]
+<references/>
-[[Category: Muravieva, T.I]]
+__TOC__
-[[Category: Zhukhlistova, N.E]]
+</StructureSection>
+[[Category: Escherichia coli]]
+[[Category: Large Structures]]
+[[Category: Abramchik YA]]
+[[Category: Esipov RS]]
+[[Category: Iaroslavtceva AK]]
+[[Category: Kuranova IP]]
+[[Category: Muravieva TI]]
+[[Category: Stepanenko VN]]
+[[Category: Timofeev VI]]
+[[Category: Zhukhlistova NE]]

4s2u: Difference between revisions

Latest revision as of 12:57, 1 March 2024

Crystal structure of the Phosphorybosylpyrophosphate synthetase from E. Coli

Structural highlights

Function

References

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