The Pro region N-terminal domain provides specific interactions required for catalysis of α-lytic protease folding

Biochemistry

Volumn 41, Issue 28, 2002, Pages 8860-8867

  Cunningham, Erin L ^a   Mau, Ted ^a   Truhlar, Stephanie M E ^a   Agard, David A ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NATIVE CONFORMATION;

BACTERIA; CRYSTAL STRUCTURE; MUTAGENESIS;

ENZYMES;

BACTERIAL ENZYME; MUTANT PROTEIN; PROTEINASE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CATALYST; CONTROLLED STUDY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SYNTHESIS; MUTATIONAL ANALYSIS; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CALORIMETRY; CATALYSIS; CIRCULAR DICHROISM; ENZYME PRECURSORS; ESCHERICHIA COLI; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SERINE ENDOPEPTIDASES;

BACTERIA (MICROORGANISMS);

EID: 0037118670     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi020214o     Document Type: Article

References (22)

1. Molecular structure of the alpha-lytic protease from myxobacter 495 at 2 Å resolution
2. Analysis of prepro-α-lytic protease expression in Escherichia coli reveals that the pro region is required for activity
3. The α-lytic protease proregion does not require a physical linkage to activate the protease domain in vivo
4. A protein-folding reaction under kinetic control
5. Unfolded conformations of alpha-lytic protease are more stable than its native state
6. Energetic landscape of α-lytic protease optimizes longevity through kinetic stability
7. Pro region C-terminus: Protease active site interactions are critical in catalyzing the folding of alpha-lytic protease
8. Pro region inhibition by steric occlusion of the α-lytic protease active site
9. Structure of alpha-lytic protease complexed with its pro region
10. Kinetic stability as a mechanism for protease longevity
11. Two energetically disparate folding pathways of α-lytic protease share a single transition state
12. Carbon nuclear magnetic resonance studies of the histidine residue in alpha-lytic protease. Implications for the catalytic mechanism of serine proteases
13. Kinetic and structural characterization of muations of glycine 216 in α-lytic protease: A new target for engineering substrate specificity
14. Determination and analysis of urea and guanidine hydrochloride denaturation curves
15. Alpha-lytic protease precursor: Characterization of a structured folding intermediate
16. Protease pro region required for folding is a potent inhibitor of the mature enzyme
17. Molscript: A program to produce both detailed and schematic plots of macromolecular structures
18. Raster 3D: Photorealistic molecular graphics
19. Correct folding of α-lytic protease is required for its extracellular secretion from Escherichia coli
20. Streptomyces griseus protease B: Secretion correlates with the length of the pro peptide