1gt9 Citations

The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase.

Structure 10 865-76 (2002)
Related entries: 1gtl, 1gtg, 1gtj

Cited: 19 times
EuropePMC logo PMID: 12057200

Abstract

Kumamolysin is a thermostable endopeptidase from Bacillus novosp. MN-32, exhibiting maximal proteolytic activity around pH 3. It belongs to the newly identified family of serine-carboxyl proteinases, which also includes CLN2, a human lysosomal homolog recently implicated in a fatal neurodegenerative disease. Kumamolysin and its complexes with two aldehyde inhibitors were crystallized, and their three-dimensional structures were solved and refined with X-ray data to 1.4 A resolution. As its Pseudomonas homolog, kumamolysin exhibits a Ser/Glu/Asp catalytic triad with particularly short interconnecting hydrogen bonds and an oxyanion hole enabling the reactive serine to attack substrate peptide bonds at quite acidic pH. An additional Glu/Trp pair, unique to kumamolysin, might further facilitate proton delocalization during nucleophilic attack, in particular at high temperature.

Articles - 1gt9 mentioned but not cited (1)

  1. Relating destabilizing regions to known functional sites in proteins. Dessailly BH, Lensink MF, Wodak SJ. BMC Bioinformatics 8 141 (2007)


Reviews citing this publication (2)

Articles citing this publication (16)

  1. Proprotein convertase models based on the crystal structures of furin and kexin: explanation of their specificity. Henrich S, Lindberg I, Bode W, Than ME. J. Mol. Biol. 345 211-227 (2005)
  2. Structures of an MHC class I molecule from B21 chickens illustrate promiscuous peptide binding. Koch M, Camp S, Collen T, Avila D, Salomonsen J, Wallny HJ, van Hateren A, Hunt L, Jacob JP, Johnston F, Marston DA, Shaw I, Dunbar PR, Cerundolo V, Jones EY, Kaufman J. Immunity 27 885-899 (2007)
  3. 1.2 A crystal structure of the serine carboxyl proteinase pro-kumamolisin; structure of an intact pro-subtilase. Comellas-Bigler M, Maskos K, Huber R, Oyama H, Oda K, Bode W. Structure 12 1313-1323 (2004)
  4. Evolution of prokaryotic subtilases: genome-wide analysis reveals novel subfamilies with different catalytic residues. Siezen RJ, Renckens B, Boekhorst J. Proteins 67 681-694 (2007)
  5. A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases. Wlodawer A, Durell SR, Li M, Oyama H, Oda K, Dunn BM. BMC Struct. Biol. 3 8 (2003)
  6. The QM/MM molecular dynamics and free energy simulations of the acylation reaction catalyzed by the serine-carboxyl peptidase kumamolisin-As. Xu Q, Guo HB, Wlodawer A, Nakayama T, Guo H. Biochemistry 46 3784-3792 (2007)
  7. Ser475, Glu272, Asp276, Asp327, and Asp360 are involved in catalytic activity of human tripeptidyl-peptidase I. Walus M, Kida E, Wisniewski KE, Golabek AA. FEBS Lett. 579 1383-1388 (2005)
  8. Aorsin, a novel serine proteinase with trypsin-like specificity at acidic pH. Lee BR, Furukawa M, Yamashita K, Kanasugi Y, Kawabata C, Hirano K, Ando K, Ichishima E. Biochem. J. 371 541-548 (2003)
  9. Structural and enzymatic characterization of physarolisin (formerly physaropepsin) proves that it is a unique serine-carboxyl proteinase. Nishii W, Ueki T, Miyashita R, Kojima M, Kim YT, Sasaki N, Murakami-Murofushi K, Takahashi K. Biochem. Biophys. Res. Commun. 301 1023-1029 (2003)
  10. Regulation of an intracellular subtilisin protease activity by a short propeptide sequence through an original combined dual mechanism. Gamble M, Künze G, Dodson EJ, Wilson KS, Jones DD. Proc. Natl. Acad. Sci. U.S.A. 108 3536-3541 (2011)
  11. Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate. Wlodawer A, Li M, Gustchina A, Oyama H, Oda K, Beyer BB, Clemente J, Dunn BM. Biochem. Biophys. Res. Commun. 314 638-645 (2004)
  12. Processing, catalytic activity and crystal structures of kumamolisin-As with an engineered active site. Okubo A, Li M, Ashida M, Oyama H, Gustchina A, Oda K, Dunn BM, Wlodawer A, Nakayama T. FEBS J. 273 2563-2576 (2006)
  13. Grifolisin, a member of the sedolisin family produced by the fungus Grifola frondosa. Suzuki N, Nishibori K, Oodaira Y, Kitamura S, Michigami K, Nagata K, Tatara Y, Lee BR, Ichishima E. Phytochemistry 66 983-990 (2005)
  14. News How to kill an enzyme (in more ways than one). Wlodawer A. Structure 12 1117-1119 (2004)
  15. Understanding the autocatalytic process of pro-kumamolisin activation from molecular dynamics and quantum mechanical/molecular mechanical (QM/MM) free-energy simulations. Yao J, Wlodawer A, Guo H. Chemistry 19 10849-10852 (2013)
  16. A tripeptidyl peptidase 1 is a binding partner of the Golgi pH regulator (GPHR) in Dictyostelium. Stumpf M, Müller R, Gaßen B, Wehrstedt R, Fey P, Karow MA, Eichinger L, Glöckner G, Noegel AA. Dis Model Mech 10 897-907 (2017)