1pya Citations

Refined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a.

J. Mol. Biol. 230 516-28 (1993)
Cited: 15 times
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The crystal structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a has been refined to an R-value of 0.15 (for the 5.0 to 2.5 A resolution shell) and 0.17 (for the 10.0 to 2.5 A resolution shell). A description of the overall structure is presented, focusing on secondary structure and subunit association. The enzyme is a hexamer of alpha beta subunits. Separate alpha and beta-chains arise from an autocatalytic cleavage reaction between two serine residues, which results in the pyruvoyl cofactor. The central core of the alpha beta subunit is a beta-sandwich which consists of two face-to-face three-stranded antiparallel beta-sheets, flanked by alpha-helices on each side. The beta-sandwich creates a stable fold that allows conformational strain to be introduced across an internal cleavage region between the alpha and beta chains and places the pyruvoyl cofactor in a position for efficient electron withdrawal from the substrate. Three alpha beta subunits are related by a molecular three-fold symmetry axis to form a trimer whose interfaces have complementary surfaces and extensive molecular interactions. Each of the interfaces contains an active site and a solvent channel that leads from the active site to the exterior of the molecule. The trimers are related by a crystallographic two-fold symmetry axis to form the hexamer with an overall dumbbell shape. The interface between trimers has few molecular interactions.

Articles - 1pya mentioned but not cited (1)

  1. Threonine 57 is required for the post-translational activation of Escherichia coli aspartate α-decarboxylase. Webb ME, Yorke BA, Kershaw T, Lovelock S, Lobley CM, Kilkenny ML, Smith AG, Blundell TL, Pearson AR, Abell C. Acta Crystallogr. D Biol. Crystallogr. 70 1166-1172 (2014)

Reviews citing this publication (4)

  1. The PLP cofactor: lessons from studies on model reactions. Richard JP, Amyes TL, Crugeiras J, Rios A. Biochim. Biophys. Acta 1814 1419-1425 (2011)
  2. Methylidene-imidazolone: a novel electrophile for substrate activation. Poppe L. Curr Opin Chem Biol 5 512-524 (2001)
  3. Novel cofactors via post-translational modifications of enzyme active sites. Okeley NM, van der Donk WA. Chem. Biol. 7 R159-71 (2000)
  4. Structural trees for protein superfamilies. Efimov AV. Proteins 28 241-260 (1997)

Articles citing this publication (10)

  1. Structural insights into the mechanism of intramolecular proteolysis. Xu Q, Buckley D, Guan C, Guo HC. Cell 98 651-661 (1999)
  2. The DmpA aminopeptidase from Ochrobactrum anthropi LMG7991 is the prototype of a new terminal nucleophile hydrolase family. Fanuel L, Goffin C, Cheggour A, Devreese B, Van Driessche G, Joris B, Van Beeumen J, Frère JM. Biochem. J. 341 ( Pt 1) 147-155 (1999)
  3. The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold. Ekstrom JL, Mathews II, Stanley BA, Pegg AE, Ealick SE. Structure 7 583-595 (1999)
  4. pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a. Schelp E, Worley S, Monzingo AF, Ernst S, Robertus JD. J. Mol. Biol. 306 727-732 (2001)
  5. SEA domain autoproteolysis accelerated by conformational strain: mechanistic aspects. Johansson DG, Macao B, Sandberg A, Härd T. J. Mol. Biol. 377 1130-1143 (2008)
  6. Characterization of the histidine decarboxylase gene of Staphylococcus epidermidis TYH1 coded on the staphylococcal cassette chromosome. Yokoi KJ, Harada Y, Shozen K, Satomi M, Taketo A, Kodaira K. Gene 477 32-41 (2011)
  7. Structure and cooperativity of a T-state mutant of histidine decarboxylase from Lactobacillus 30a. Worley S, Schelp E, Monzingo AF, Ernst S, Robertus JD. Proteins 46 321-329 (2002)
  8. Determinants of histamine recognition: implications for the design of antihistamines. Konkimalla VB, Chandra N. Biochem. Biophys. Res. Commun. 309 425-431 (2003)
  9. Potential folding-function interrelationship in proteins. Barzilai A, Kumar S, Wolfson H, Nussinov R. Proteins 56 635-649 (2004)
  10. Up-regulation of histidine decarboxylase expression and histamine content in B16F10 murine melanoma cells. Davis SC, Clark S, Hayes JR, Green TL, Gruetter CA. Inflamm. Res. 60 55-61 (2011)

Related citations provided by authors (4)

  1. Pyruvoyl-Dependent Histidine Decarboxylase: Active Site Structure and Mechanistic Analysis. Gallagher T, Snell EE, Hackert ML J. Biol. Chem. 264 12737- (1989)
  2. Structure Determination of Histidine Decarboxylase from Lactobacillus 30A at 3.0 Angstroms Resolution. Parks EH, Ernst SR, Hamlin R, Xuong NH, Hackert ML J. Mol. Biol. 182 455- (1985)
  3. The Molecular Symmetry of Histidine Decarboxylase and Prohistidine Decarboxylase by Rotation Function Analysis. Parks EH, Clinger K, Hackert ML Acta Crystallogr., B 39 490- (1983)
  4. Crystallization and Subunit Structure of Histidine Decarboxylase from Lactobacillus 30A. Hackert ML, Meador WE, Oliver RM, Salmon JB, Rescei PA, Snell EE J. Biol. Chem. 256 687- (1981)