1nhc › Citations

Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger.

van Pouderoyen G, Snijder HJ, Benen JA, Dijkstra BW
FEBS Lett 554 462-6 (2003)
Cited: 43 times
EuropePMC logo PMID: 14623112

Abstract

Endopolygalacturonase I is a processive enzyme, while the 60% sequence identical endopolygalacturonase II is not. The 1.70 A resolution crystal structure of endopolygalacturonase I reveals a narrowed substrate binding cleft. In addition, Arg96, a residue in this cleft previously shown to be critical for processivity, interacts with the substrate mimics glycerol and sulfate in several well-defined conformations in the six molecules in the asymmetric unit. From this we conclude that both Arg96 and the narrowed substrate binding cleft contribute to retaining the substrate while it moves through the active site after a cleavage event has occurred.

Articles - 1nhc mentioned but not cited (7)

  1. Pi-Pi contacts are an overlooked protein feature relevant to phase separation. Vernon RM, Chong PA, Tsang B, Kim TH, Bah A, Farber P, Lin H, Forman-Kay JD. Elife 7 e31486 (2018)
  2. New Insights into the Role of T3 Loop in Determining Catalytic Efficiency of GH28 Endo-Polygalacturonases. Tu T, Meng K, Luo H, Turunen O, Zhang L, Cheng Y, Su X, Ma R, Shi P, Wang Y, Yang P, Yao B. PLoS One 10 e0135413 (2015)
  3. Nanotechnology enabled enhancement of enzyme activity and thermostability: study on impaired pectate lyase from attenuated Macrophomina phaseolina in presence of hydroxyapatite nanoparticle. Dutta N, Mukhopadhyay A, Dasgupta AK, Chakrabarti K. PLoS One 8 e63567 (2013)
  4. Study of the mode of action of a polygalacturonase from the phytopathogen Burkholderia cepacia. Massa C, Clausen MH, Stojan J, Lamba D, Campa C. Biochem J 407 207-217 (2007)
  5. Functional Classification and Characterization of the Fungal Glycoside Hydrolase 28 Protein Family. Villarreal F, Stocchi N, Ten Have A. J Fungi (Basel) 8 217 (2022)
  6. Crystallization, X-ray diffraction analysis and preliminary structure determination of the polygalacturonase PehA from Agrobacterium vitis. Vordtriede PB, Yoder MD. Acta Crystallogr Sect F Struct Biol Cryst Commun 64 645-647 (2008)
  7. The Synthesis, Fungicidal Activity, and in Silico Study of Alkoxy Analogues of Natural Precocenes I, II, and III. Ramadan KMA, El-Beltagi HS, Iqbal Z, Bendary ESA. Molecules 27 7177 (2022)


Reviews citing this publication (4)

  1. Fungal enzyme sets for plant polysaccharide degradation. van den Brink J, de Vries RP. Appl Microbiol Biotechnol 91 1477-1492 (2011)
  2. Homogalacturonan-modifying enzymes: structure, expression, and roles in plants. Sénéchal F, Wattier C, Rustérucci C, Pelloux J. J Exp Bot 65 5125-5160 (2014)
  3. Cold active pectinases: advancing the food industry to the next generation. Adapa V, Ramya LN, Pulicherla KK, Rao KR. Appl Biochem Biotechnol 172 2324-2337 (2014)
  4. Pectins, Endopolygalacturonases, and Bioenergy. Latarullo MB, Tavares EQ, Maldonado GP, Leite DC, Buckeridge MS. Front Plant Sci 7 1401 (2016)

Articles citing this publication (32)



Quick links