5enl › Citations

Inhibition of enolase: the crystal structures of enolase-Ca2(+)- 2-phosphoglycerate and enolase-Zn2(+)-phosphoglycolate complexes at 2.2-A resolution.

Lebioda L, Stec B, Brewer JM, Tykarska E
Biochemistry 30 2823-7 (1991)
Cited: 23 times
EuropePMC logo PMID: 2007121

Abstract

Enolase is a metalloenzyme which catalyzes the elimination of H2O from 2-phosphoglyceric acid (PGA) to form phosphoenolpyruvate (PEP). Mg2+ and Zn2+ are cofactors which strongly bind and activate the enzyme. Ca2+ also binds strongly but does not produce activity. Phosphoglycolate (PG) is a competitive inhibitor of enolase. The structures of two inhibitory ternary complexes: yeast enolase-Ca2(+)-PGA and yeast enolase-Zn2(+)-PG, were determined by X-ray diffraction to 2.2-A resolution and were refined by crystallographic least-squares to R = 14.8% and 15.7%, respectively, with good geometries of the models. These structures are compared with the structure of the precatalytic ternary complex enolase-Mg2(+)-PGA/PEP (Lebioda & Stec, 1991). In the complex enolase-Ca2(+)-PGA, the PGA molecule coordinates to the Ca2+ ion with the hydroxyl group, as in the precatalytic complex. The conformation of the PGA molecule is however different. In the active complex, the organic part of the PGA molecule is planar, similar to the product. In the inhibitory complex, the carboxylic group is in an orthonormal conformation. In the inhibitory complex enolase-Zn2(+)-PG, the PG molecule coordinates with the carboxylic group in a monodentate mode. In both inhibitory complexes, the conformational changes in flexible loops, which were observed in the precatalytic complex, do not take place. The lack of catalytic metal ion binding suggests that these conformational changes are necessary for the formation of the catalytic metal ion binding site.

Articles - 5enl mentioned but not cited (4)

  1. The Catalytic Site Atlas: a resource of catalytic sites and residues identified in enzymes using structural data. Porter CT, Bartlett GJ, Thornton JM. Nucleic Acids Res 32 D129-33 (2004)
  2. Alignment of protein sequences by their profiles. Marti-Renom MA, Madhusudhan MS, Sali A. Protein Sci 13 1071-1087 (2004)
  3. Development of quantitative structure-binding affinity relationship models based on novel geometrical chemical descriptors of the protein-ligand interfaces. Zhang S, Golbraikh A, Tropsha A. J Med Chem 49 2713-2724 (2006)
  4. ResBoost: characterizing and predicting catalytic residues in enzymes. Alterovitz R, Arvey A, Sankararaman S, Dallett C, Freund Y, Sjölander K. BMC Bioinformatics 10 197 (2009)


Reviews citing this publication (2)

  1. A structural role for arginine in proteins: multiple hydrogen bonds to backbone carbonyl oxygens. Borders CL, Broadwater JA, Bekeny PA, Salmon JE, Lee AS, Eldridge AM, Pett VB. Protein Sci 3 541-548 (1994)
  2. Combining structural genomics and enzymology: completing the picture in metabolic pathways and enzyme active sites. Erlandsen H, Abola EE, Stevens RC. Curr Opin Struct Biol 10 719-730 (2000)

Articles citing this publication (17)

  1. Catalysing new reactions during evolution: economy of residues and mechanism. Bartlett GJ, Borkakoti N, Thornton JM. J Mol Biol 331 829-860 (2003)
  2. Superfamily active site templates. Meng EC, Polacco BJ, Babbitt PC. Proteins 55 962-976 (2004)
  3. Structure of 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: comparison of the Mn(2+)*2-phosphoglycolate and the Pb(2+)*2-phosphoenolpyruvate complexes and implications for catalysis. Wagner T, Shumilin IA, Bauerle R, Kretsinger RH. J Mol Biol 301 389-399 (2000)
  4. The crystal structure of Trypanosoma brucei enolase: visualisation of the inhibitory metal binding site III and potential as target for selective, irreversible inhibition. da Silva Giotto MT, Hannaert V, Vertommen D, de A S Navarro MV, Rider MH, Michels PA, Garratt RC, Rigden DJ. J Mol Biol 331 653-665 (2003)
  5. Use of Relibase for retrieving complex three-dimensional interaction patterns including crystallographic packing effects. Bergner A, Günther J, Hendlich M, Klebe G, Verdonk M. Biopolymers 61 99-110 (2001)
  6. High-performance prediction of functional residues in proteins with machine learning and computed input features. Somarowthu S, Yang H, Hildebrand DG, Ondrechen MJ. Biopolymers 95 390-400 (2011)
  7. Fluoride inhibition of yeast enolase: crystal structure of the enolase-Mg(2+)-F(-)-Pi complex at 2.6 A resolution. Lebioda L, Zhang E, Lewinski K, Brewer JM. Proteins 16 219-225 (1993)
  8. Molecular speciation and tissue compartmentation of zinc in durum wheat grains with contrasting nutritional status. Persson DP, de Bang TC, Pedas PR, Kutman UB, Cakmak I, Andersen B, Finnie C, Schjoerring JK, Husted S. New Phytol 211 1255-1265 (2016)
  9. The enolases of ice plant and Arabidopsis contain a potential disulphide and are redox sensitive. Anderson LE, Li AD, Stevens FJ. Phytochemistry 47 707-713 (1998)
  10. A Moonlighting Enolase from Lactobacillus gasseri does not Require Enzymatic Activity to Inhibit Neisseria gonorrhoeae Adherence to Epithelial Cells. Spurbeck RR, Harris PT, Raghunathan K, Arvidson DN, Arvidson CG. Probiotics Antimicrob Proteins 7 193-202 (2015)
  11. Structure analysis of Entamoeba histolytica enolase. Schulz EC, Tietzel M, Tovy A, Ankri S, Ficner R. Acta Crystallogr D Biol Crystallogr 67 619-627 (2011)
  12. A proteomic approach to identify metalloproteins and metal-binding proteins in liver from diabetic rats. Braga CP, Vieira JCS, Grove RA, Boone CHT, Leite AL, Buzalaf MAR, Fernandes AAH, Adamec J, Padilha PM. Int J Biol Macromol 96 817-832 (2017)
  13. Biochemical and Structural Characterization of Enolase from Chloroflexus aurantiacus: Evidence for a Thermophilic Origin. Zadvornyy OA, Boyd ES, Posewitz MC, Zorin NA, Peters JW. Front Bioeng Biotechnol 3 74 (2015)
  14. Crystal structure of an efficacious gonococcal adherence inhibitor: an enolase from Lactobacillus gasseri. Raghunathan K, Harris PT, Spurbeck RR, Arvidson CG, Arvidson DN. FEBS Lett 588 2212-2216 (2014)
  15. A differential scanning calorimetric study of the effects of metal ions, substrate/product, substrate analogues and chaotropic anions on the thermal denaturation of yeast enolase 1. Brewer JM, Wampler JE. Int J Biol Macromol 28 213-218 (2001)
  16. Functional and structural basis of E. coli enolase inhibition by SF2312: a mimic of the carbanion intermediate. Krucinska J, Lombardo MN, Erlandsen H, Hazeen A, Duay SS, Pattis JG, Robinson VL, May ER, Wright DL. Sci Rep 9 17106 (2019)
  17. Immunolocation and enzyme activity analysis of Cryptosporidium parvum enolase. Mi R, Yang X, Huang Y, Cheng L, Lu K, Han X, Chen Z. Parasit Vectors 10 273 (2017)


Related citations provided by authors (6)

  1. Mechanism of Enolase: The Crystal Structure of Enolase-Mg2+-Phosphoglycerate(Slash) Phosphoenolpyruvate Complex at 2.2-Angstroms Resolution. Lebioda L, Stec B Biochemistry 30 2817- (1991)
  2. Refined Structure of Yeast Apo-Enolase at 2.25 Angstroms Resolution. Stec B, Lebioda L J. Mol. Biol. 211 235- (1990)
  3. Crystal Structure of Holoenzyme Refined at 1.9 Angstroms Resolution: Trigonal-Bipyramidal Geometry of the Cation Binding Site. Lebioda L, Stec B J. Am. Chem. Soc. 111 8511- (1989)
  4. The Structure of Yeast Enolase at 2.25-Angstroms Resolution. An 8-Fold Beta+Alpha-Barrel with a Novel Beta Beta Alpha Alpha (Beta Alpha)6 Topology. Lebioda L, Stec B, Brewer JM J. Biol. Chem. 264 3685- (1989)
  5. Crystal Structure of Enolase Indicates that Enolase and Pyruvate Kinase Evolved from a Common Ancestor. Lebioda L, Stec B Nature 333 683- (1988)
  6. Crystallization and Preliminary Crystallographic Data for a Tetragonal Form of Yeast Enolase. Lebioda L, Brewer JM J. Mol. Biol. 180 213- (1984)

Quick links