2jzn › Citations

Solution NMR structures of productive and non-productive complexes between the A and B domains of the cytoplasmic subunit of the mannose transporter of the Escherichia coli phosphotransferase system.

Hu J, Hu K, Williams DC, Komlosh ME, Cai M, Clore GM
J Biol Chem 283 11024-37 (2008)
Related entries: 1vsq, 2jzh, 2jzo

Cited: 18 times
EuropePMC logo PMID: 18270202

Abstract

Solution structures of complexes between the isolated A (IIA(Man)) and B (IIB(Man)) domains of the cytoplasmic component of the mannose transporter of Escherichia coli have been solved by NMR. The complex of wild-type IIA(Man) and IIB(Man) is a mixture of two species comprising a productive, phosphoryl transfer competent complex and a non-productive complex with the two active site histidines, His-10 of IIA(Man) and His-175 of IIB(Man), separated by approximately 25A. Mutation of the active site histidine, His-10, of IIA(Man) to a glutamate, to mimic phosphorylation, results in the formation of a single productive complex. The apparent equilibrium dissociation constants for the binding of both wild-type and H10E IIA(Man) to IIB(Man) are approximately the same (K(D) approximately 0.5 mM). The productive complex can readily accommodate a transition state involving a pentacoordinate phosphoryl group with trigonal bipyramidal geometry bonded to the Nepsilon2 atom of His-10 of IIA(Man) and the Ndelta1 atom of His-175 of IIB(Man) with negligible (<0.2A) local backbone conformational changes in the immediate vicinity of the active site. The non-productive complex is related to the productive one by a approximately 90 degrees rotation and approximately 37A translation of IIB(Man) relative to IIA(Man), leaving the active site His-175 of IIB(Man) fully exposed to solvent in the non-productive complex. The interaction surface on IIA(Man) for the non-productive complex comprises a subset of residues used in the productive complex and in both cases involves both subunits of IIA(Man). The selection of the productive complex by IIA(Man)(H10E) can be attributed to neutralization of the positively charged Arg-172 of IIB(Man) at the center of the interface. The non-productive IIA(Man)-IIB(Man) complex may possibly be relevant to subsequent phosphoryl transfer from His-175 of IIB(Man) to the incoming sugar located on the transmembrane IIC(Man)-IID(Man) complex.

Articles - 2jzn mentioned but not cited (1)

  1. Forcefield_PTM: Ab Initio Charge and AMBER Forcefield Parameters for Frequently Occurring Post-Translational Modifications. Khoury GA, Thompson JP, Smadbeck J, Kieslich CA, Floudas CA. J Chem Theory Comput 9 5653-5674 (2013)


Reviews citing this publication (4)

  1. Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes. Clore GM, Iwahara J. Chem Rev 109 4108-4139 (2009)
  2. NMR approaches for structural analysis of multidomain proteins and complexes in solution. Göbl C, Madl T, Simon B, Sattler M. Prog Nucl Magn Reson Spectrosc 80 26-63 (2014)
  3. Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Clore GM, Venditti V. Trends Biochem Sci 38 515-530 (2013)
  4. 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 (13)

  1. Replica exchange simulations of transient encounter complexes in protein-protein association. Kim YC, Tang C, Clore GM, Hummer G. Proc Natl Acad Sci U S A 105 12855-12860 (2008)
  2. Solution structure of a complex of the histidine autokinase CheA with its substrate CheY. Mo G, Zhou H, Kawamura T, Dahlquist FW. Biochemistry 51 3786-3798 (2012)
  3. Molecular simulations of a dynamic protein complex: role of salt-bridges and polar interactions in configurational transitions. Zhang L, Buck M. Biophys J 105 2412-2417 (2013)
  4. Mono-dimensional blue native-PAGE and bi-dimensional blue native/urea-PAGE or/SDS-PAGE combined with nLC-ESI-LIT-MS/MS unveil membrane protein heteromeric and homomeric complexes in Streptococcus thermophilus. Salzano AM, Novi G, Arioli S, Corona S, Mora D, Scaloni A. J Proteomics 94 240-261 (2013)
  5. Crystal structures of phosphotransferase system enzymes PtxB (IIB(Asc)) and PtxA (IIA(Asc)) from Streptococcus mutans. Lei J, Li LF, Su XD. J Mol Biol 386 465-475 (2009)
  6. Solution structure of the IIAChitobiose-HPr complex of the N,N'-diacetylchitobiose branch of the Escherichia coli phosphotransferase system. Jung YS, Cai M, Clore GM. J Biol Chem 287 23819-23829 (2012)
  7. Solution structure of the IIAChitobiose-IIBChitobiose complex of the N,N'-diacetylchitobiose branch of the Escherichia coli phosphotransferase system. Jung YS, Cai M, Clore GM. J Biol Chem 285 4173-4184 (2010)
  8. Activity of the Enterococcus faecalis EIIA(gnt) PTS component and its strong interaction with EIIB(gnt). Brockmeier A, Skopnik M, Koch B, Herrmann C, Hengstenberg W, Welti S, Scheffzek K. Biochem Biophys Res Commun 388 630-636 (2009)
  9. Structural characterization of the PTS IIA and IIB proteins associated with pneumococcal fucose utilization. Higgins MA, Hamilton AM, Boraston AB. Proteins 85 963-968 (2017)
  10. Structure of the Enterococcus faecalis EIIA(gnt) PTS component. Reinelt S, Koch B, Hothorn M, Hengstenberg W, Welti S, Scheffzek K. Biochem Biophys Res Commun 388 626-629 (2009)
  11. Streptococcal phosphotransferase system imports unsaturated hyaluronan disaccharide derived from host extracellular matrices. Oiki S, Nakamichi Y, Maruyama Y, Mikami B, Murata K, Hashimoto W. PLoS One 14 e0224753 (2019)
  12. Biophysical characterization of the domain association between cytosolic A and B domains of the mannitol transporter enzymes II(Mtl) in the presence and absence of a connecting linker. Lee KO, Kim EH, Kim G, Jung JY, Katayama S, Nakamura S, Suh JY. Protein Sci 25 1803-1811 (2016)
  13. Crystal Structure of Mannose Specific IIA Subunit of Phosphotransferase System from Streptococcus pneumoniae. Magoch M, Nogly P, Grudnik P, Ma P, Boczkus B, Neves AR, Archer M, Dubin G. Molecules 25 (2020)


Quick links