Sequence analysis and crystal structure of a glycosylated protease from Euphorbia resinifera latex for its proteolytic activity aspect

2021 ◽  
Author(s):  
Jaruwan Siritapetawee ◽  
Jakrada Attarataya ◽  
Ratana Charoenwattanasatien
Keyword(s):  
Crystal Structure ◽  
Sequence Analysis ◽  
Proteolytic Activity

Crystal structure and specific location of a germin-like protein with proteolytic activity from Thevetia peruviana

Plant Science ◽  
2020 ◽  
Vol 298 ◽  
pp. 110590
Author(s):  
Wallace T. Cruz ◽  
Eduardo H.S. Bezerra ◽  
Márcio V. Ramos ◽  
Bruno A.M. Rocha ◽  
Maria C. Medina ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Proteolytic Activity ◽  
Specific Location ◽  
Thevetia Peruviana

Cloning, sequence analysis and crystal structure determination of a miraculin-like protein from Murraya koenigii

2010 ◽  
Vol 494 (1) ◽  
pp. 15-22 ◽  
Author(s):  
Deepankar Gahloth ◽  
Purushotham Selvakumar ◽  
Chandan Shee ◽  
Pravindra Kumar ◽  
Ashwani Kumar Sharma
Keyword(s):  
Crystal Structure ◽  
Sequence Analysis ◽  
Structure Determination ◽  
Crystal Structure Determination ◽  
Murraya Koenigii

scholarly journals cDNA cloning and sequence analysis of human pancreatic procarboxypeptidase A1

1992 ◽  
Vol 287 (1) ◽  
pp. 299-303 ◽  
Author(s):  
L Catasús ◽  
V Villegas ◽  
R Pascual ◽  
F X Avilés ◽  
C Wicker-Planquart ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acids ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Central Region ◽  
Polyclonal Antibodies ◽  
Amino Acid Sequences ◽  
Sequence Comparisons ◽  
Activation Segment ◽  
Flanking Regions

Using polyclonal antibodies raised against human pancreatic procarboxypeptidases, a full-length cDNA coding for an A-type proenzyme was isolated from a lambda gt11 human pancreatic library. This cDNA contains standard 3′ and 5′ flanking regions, a poly(A)+ tail and a central region of 1260 nucleotides coding for a protein of 419 amino acids. On the basis of sequence comparisons, the human protein was classified as a procarboxypeptidase A1 which is very similar to the previously described A1 forms from rat and bovine pancreatic glands. The presence of the amino acid sequences assumed to be of importance for the zymogen inhibition by its activation segment, primarily on the basis of the recently reported crystal structure of the B form, further supports the proposed classification.

scholarly journals Chemical modification of GSH transferase P1-1 confirms the presence of Arg-13, Lys-44 and one carboxylate group in the GSH-binding domain of the active site

1993 ◽  
Vol 293 (2) ◽  
pp. 357-362 ◽  
Author(s):  
C Xia ◽  
D J Meyer ◽  
H Chen ◽  
P Reinemer ◽  
R Huber ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Sequence Analysis ◽  
Active Site ◽  
Sequence Similarity ◽  
Lysine Residue ◽  
Carboxylate Group ◽  
Terminal Sequence ◽  
Crystallographic Study ◽  
Binding Determinants ◽  
Subunit B

GSH transferase P1-1 (GSTP1-1) was modified with group-specific reagents. Kinetic experiments demonstrated that inactivation of GSTP1-1 occurred upon reaction of one arginine residue per subunit with diacetyl, one lysine residue per subunit with 2,4,6-trinitrobenzene sulphonate, or one carboxylate group per subunit with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide. All three inactivation reactions were inhibited by compounds known to bind at the GSH site of the enzyme but were unaffected by the electrophile 1-chloro-2,4-dinitrobenzene. N-terminal sequence analysis showed that Arg-13 was modified by diacetyl and that this modification was inhibited by GSH. Arg-11 was not modified. The lysine residue modified by 2,4,6-trinitrobenzene sulphonate and protected by S-octylglutathione was identified as Lys-44 by sequencing of tryptic peptides. The findings are in agreement with the involvement of Arg-13 and Lys-44 in binding of GSH, as determined from the crystal structure [Reinemer, Dirr, Ladenstein, Huber, Lo Bello, Frederici and Parker (1992) J. Mol. Biol. 227, 214-226]. The present data also implicate a single carboxylate in GSH binding, consistent with the involvement of Asp-98 of subunit B determined from the crystallographic study. The GSH-binding determinants of GSTP1-1 are compared using sequence similarity with those of GSTs of Alpha, Mu and Theta classes.

scholarly journals Actin mutations that show suppression with fimbrin mutations identify a likely fimbrin-binding site on actin.

1994 ◽  
Vol 126 (2) ◽  
pp. 413-422 ◽  
Author(s):  
J E Honts ◽  
T S Sandrock ◽  
S M Brower ◽  
J L O'Dell ◽  
A E Adams
Keyword(s):  
Crystal Structure ◽  
Sequence Analysis ◽  
Binding Site ◽  
Actin Filaments ◽  
Biochemical Analysis ◽  
Actin Binding ◽  
Cross Linking ◽  
Temperature Sensitive ◽  
Small Domain

Actin interacts with a large number of different proteins that modulate its assembly and mediate its functions. One such protein is the yeast actin-binding protein Sac6p, which is homologous to vertebrate fimbrin (Adams, A. E. M., D. Botstein, and D. G. Drubin. 1991. Nature (Lond.). 354:404-408.). Sac6p was originally identified both genetically (Adams, A. E. M., and D. Botstein. 1989. Genetics. 121:675-683.) by dominant, reciprocal suppression of a temperature-sensitive yeast actin mutation (act1-1), as well as biochemically (Drubin, D. G., K. G. Miller, and D. Botstein. 1988. J. Cell Biol. 107: 2551-2561.). To identify the region on actin that interacts with Sac6p, we have analyzed eight different act1 mutations that show suppression with sac6 mutant alleles, and have asked whether (a) these mutations occur in a small defined region on the crystal structure of actin; and (b) the mutant actins are defective in their interaction with Sac6p in vitro. Sequence analysis indicates that all of these mutations change residues that cluster in the small domain of the actin crystal structure, suggesting that this region is an important part of the Sac6p-binding domain. Biochemical analysis reveals defects in the ability of several of the mutant actins to bind Sac6p, and a reduction in Sac6p-induced cross-linking of mutant actin filaments. Together, these observations identify a likely site of interaction of fimbrin on actin.

X-ray crystal structure of CMS1MS2: a high proteolytic activity cysteine proteinase from Carica candamarcensis

Amino Acids ◽  
2012 ◽  
Vol 43 (6) ◽  
pp. 2381-2391 ◽  
Author(s):  
Marco T. R. Gomes ◽  
Raphael D. Teixeira ◽  
Míriam T. P. Lopes ◽  
Ronaldo A. P. Nagem ◽  
Carlos E. Salas
Keyword(s):  
Crystal Structure ◽  
Proteolytic Activity ◽  
Cysteine Proteinase ◽  
X Ray ◽  
High Proteolytic Activity

scholarly journals Structural evidence for a latch mechanism regulating access to the active site of SufS-family cysteine desulfurases

2020 ◽  
Vol 76 (3) ◽  
pp. 291-301 ◽  
Author(s):  
Jack A. Dunkle ◽  
Michael R. Bruno ◽  
Patrick A. Frantom
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Sequence Analysis ◽  
Active Site ◽  
Resting State ◽  
Sulfur Source ◽  
Structural Elements ◽  
Cysteine Desulfurase ◽  
X Ray

Cysteine serves as the sulfur source for the biosynthesis of Fe–S clusters and thio-cofactors, molecules that are required for core metabolic processes in all organisms. Therefore, cysteine desulfurases, which mobilize sulfur for its incorporation into thio-cofactors by cleaving the Cα—S bond of cysteine, are ubiquitous in nature. SufS, a type 2 cysteine desulfurase that is present in plants and microorganisms, mobilizes sulfur from cysteine to the transpersulfurase SufE to initiate Fe–S biosynthesis. Here, a 1.5 Å resolution X-ray crystal structure of the Escherichia coli SufS homodimer is reported which adopts a state in which the two monomers are rotated relative to their resting state, displacing a β-hairpin from its typical position blocking transpersulfurase access to the SufS active site. A global structure and sequence analysis of SufS family members indicates that the active-site β-hairpin is likely to require adjacent structural elements to function as a β-latch regulating access to the SufS active site.

scholarly journals Pig heart short chain L-3-hydroxyacyl-CoA dehydrogenase revisited: Sequence analysis and crystal structure determination

1999 ◽  
Vol 8 (10) ◽  
pp. 2010-2018 ◽  
Author(s):  
Joseph J. Barycki ◽  
Laurie K. O'Brien ◽  
Jens J. Birktoft ◽  
Arnold W. Strauss ◽  
Leonard J. Banaszak
Keyword(s):  
Crystal Structure ◽  
Sequence Analysis ◽  
Structure Determination ◽  
Short Chain ◽  
Crystal Structure Determination ◽  
Hydroxyacyl Coa Dehydrogenase
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