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Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase.

Wang Y, Liu L, Wei Z, Cheng Z, Lin Y, Gong W
J Biol Chem 281 39642-8 (2006)
Related entries: 2a9j, 2f90, 2h4x, 2hhj

Cited: 21 times
EuropePMC logo PMID: 17052986

Abstract

Bisphosphoglycerate mutase is an erythrocyte-specific enzyme catalyzing a series of intermolecular phosphoryl group transfer reactions. Its main function is to synthesize 2,3-bisphosphoglycerate, the allosteric effector of hemoglobin. In this paper, we directly observed real-time motion of the enzyme active site and the substrate during phosphoryl transfer. A series of high resolution crystal structures of human bisphosphoglycerate mutase co-crystallized with 2,3-bisphosphoglycerate, representing different time points in the phosphoryl transfer reaction, were solved. These structures not only clarify the argument concerning the substrate binding mode for this enzyme family but also depict the entire process of the key histidine phosphorylation as a "slow movie". It was observed that the enzyme conformation continuously changed during the different states of the reaction. These results provide direct evidence for an "in line" phosphoryl transfer mechanism, and the roles of some key residues in the phosphoryl transfer process are identified.

Articles - 2h4z mentioned but not cited (4)

  1. Monoclonal 1- and 3-Phosphohistidine Antibodies: New Tools to Study Histidine Phosphorylation. Fuhs SR, Meisenhelder J, Aslanian A, Ma L, Zagorska A, Stankova M, Binnie A, Al-Obeidi F, Mauger J, Lemke G, Yates JR, Hunter T. Cell 162 198-210 (2015)
  2. Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC. Taylor NM, Glatt S, Hennrich ML, von Scheven G, Grötsch H, Fernández-Tornero C, Rybin V, Gavin AC, Kolb P, Müller CW. J Biol Chem 288 15110-15120 (2013)
  3. Conformation and dynamics of the C-terminal region in human phosphoglycerate mutase 1. Liu SE, Hu JC, Zhang H, Xu P, Wan W, Zheng MY, Yu KQ, Ding H, Jiang HL, Zhou L, Luo C. Acta Pharmacol Sin 38 1673-1682 (2017)
  4. Molecular insight into 2-phosphoglycolate activation of the phosphatase activity of bisphosphoglycerate mutase. Aljahdali AS, Musayev FN, Burgner JW, Ghatge MS, Shekar V, Zhang Y, Omar AM, Safo MK. Acta Crystallogr D Struct Biol 78 472-482 (2022)


Reviews citing this publication (1)

  1. The many ways that nature has exploited the unusual structural and chemical properties of phosphohistidine for use in proteins. Kalagiri R, Hunter T. Biochem J 478 3575-3596 (2021)

Articles citing this publication (16)

  1. Tyr26 phosphorylation of PGAM1 provides a metabolic advantage to tumours by stabilizing the active conformation. Hitosugi T, Zhou L, Fan J, Elf S, Zhang L, Xie J, Wang Y, Gu TL, Alečković M, LeRoy G, Kang Y, Kang HB, Seo JH, Shan C, Jin P, Gong W, Lonial S, Arellano ML, Khoury HJ, Chen GZ, Shin DM, Khuri FR, Boggon TJ, Kang S, He C, Chen J. Nat Commun 4 1790 (2013)
  2. The catalytic scaffold of the haloalkanoic acid dehalogenase enzyme superfamily acts as a mold for the trigonal bipyramidal transition state. Lu Z, Dunaway-Mariano D, Allen KN. Proc Natl Acad Sci U S A 105 5687-5692 (2008)
  3. Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate. Oslund RC, Su X, Haugbro M, Kee JM, Esposito M, David Y, Wang B, Ge E, Perlman DH, Kang Y, Muir TW, Rabinowitz JD. Nat Chem Biol 13 1081-1087 (2017)
  4. Trapping conformational states along ligand-binding dynamics of peptide deformylase: the impact of induced fit on enzyme catalysis. Fieulaine S, Boularot A, Artaud I, Desmadril M, Dardel F, Meinnel T, Giglione C. PLoS Biol 9 e1001066 (2011)
  5. Extending the Nonbonded Cationic Dummy Model to Account for Ion-Induced Dipole Interactions. Liao Q, Pabis A, Strodel B, Kamerlin SCL. J Phys Chem Lett 8 5408-5414 (2017)
  6. Structure and activity of the metal-independent fructose-1,6-bisphosphatase YK23 from Saccharomyces cerevisiae. Kuznetsova E, Xu L, Singer A, Brown G, Dong A, Flick R, Cui H, Cuff M, Joachimiak A, Savchenko A, Yakunin AF. J Biol Chem 285 21049-21059 (2010)
  7. Letter Erythrocytosis associated with a novel missense mutation in the BPGM gene. Petousi N, Copley RR, Lappin TR, Haggan SE, Bento CM, Cario H, Percy MJ, WGS Consortium, Ratcliffe PJ, Robbins PA, McMullin MF. Haematologica 99 e201-4 (2014)
  8. Structures of the phosphorylated and VO(3)-bound 2H-phosphatase domain of Sts-2. Chen Y, Jakoncic J, Parker KA, Carpino N, Nassar N. Biochemistry 48 8129-8135 (2009)
  9. An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase. Davies DR, Staker BL, Abendroth JA, Edwards TE, Hartley R, Leonard J, Kim H, Rychel AL, Hewitt SN, Myler PJ, Stewart LJ. Acta Crystallogr Sect F Struct Biol Cryst Commun 67 1044-1050 (2011)
  10. Snapshots during the catalytic cycle of a histidine acid phytase reveal an induced-fit structural mechanism. Acquistapace IM, Zi Etek MA, Li AWH, Salmon M, Kühn I, Bedford MR, Brearley CA, Hemmings AM. J Biol Chem 295 17724-17737 (2020)
  11. The change of synovial fluid proteome in rabbit surgery-induced model of knee osteoarthritis. Luo Q, Qin X, Qiu Y, Hou L, Yang N. Am J Transl Res 10 2087-2101 (2018)
  12. Unliganded structure of human bisphosphoglycerate mutase reveals side-chain movements induced by ligand binding. Patterson A, Price NC, Nairn J. Acta Crystallogr Sect F Struct Biol Cryst Commun 66 1415-1420 (2010)
  13. Insights into the phosphatase and the synthase activities of human bisphosphoglycerate mutase: a quantum mechanics/molecular mechanics simulation. Chu WT, Zheng QC, Zhang HX. Phys Chem Chem Phys 16 3946-3954 (2014)
  14. NLDB: a database for 3D protein-ligand interactions in enzymatic reactions. Murakami Y, Omori S, Kinoshita K. J Struct Funct Genomics 17 101-110 (2016)
  15. Structure of RNA 3'-phosphate cyclase bound to substrate RNA. Desai KK, Bingman CA, Cheng CL, Phillips GN, Raines RT. RNA 20 1560-1566 (2014)
  16. Most protein domains exist as variants with distinct functions across cells, tissues and diseases. Vitting-Seerup K. NAR Genom Bioinform 5 lqad084 (2023)


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