X-ray crystal structure of the bovine alpha-chymotrypsin/eglin c complex at 2.6 A resolution.

M. Bolognesi, L. Pugliese, G. Gatti, F. Frigerio, A. Coda, L. Antolini, H. P. Schnebli, E. Menegatti, G. Amiconi, P. Ascenzi

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The crystal structure of the molecular complex formed by bovine alpha-chymotrypsin and the recombinant serine proteinase inhibitor eglin c from Hirudo medicinalis has been solved using monoclinic crystals of the complex, reported previously. Four circle diffractometer data at 3.0 A resolution were employed to determine the structure by molecular replacement techniques. Bovine alpha-chymotrypsin alone was used as the search model; it allowed us to correctly orient and translate the enzyme in the unit cell and to obtain sufficient electron density for positioning the eglin c molecule. After independent rigid body refinement of the two complex components, the molecular model yielded a crystallographic R factor of 0.39. Five iterative cycles of restrained crystallographic refinement and model building were conducted, gradually increasing resolution. The current R factor at 2.6 A resolution (diffractometer data) is 0.18. The model includes 56 solvent molecules. Eglin c binds to bovine alpha-chymotrypsin in a manner consistent with other known serine proteinase/inhibitor complex structures. The reactive site loop shows the expected conformation for productive binding and is in tight contact with bovine alpha-chymotrypsin between subsites P3 and P'2; Leu 451 acts as the P1 residue, located in the primary specificity S1 site of the enzyme. Hydrogen bonds equivalent to those observed in complexes of trypsin(ogen) with the pancreatic basic- and secretory-inhibitors are found around the scissile peptide bond.

Original languageEnglish
Pages (from-to)163-168
Number of pages6
JournalJournal of molecular recognition : JMR
Volume3
Issue number4
Publication statusPublished - Aug 1990

Fingerprint

Crystal structure
X-Rays
X rays
Serine Proteinase Inhibitors
R Factors
Diffractometers
Molecular Structure
Enzymes
Hirudo medicinalis
Molecules
Molecular Models
Trypsin
Peptides
Carrier concentration
Conformations
Hydrogen
Catalytic Domain
Hydrogen bonds
Electrons
Crystals

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Molecular Biology
  • Computer Vision and Pattern Recognition
  • Immunology

Cite this

Bolognesi, M., Pugliese, L., Gatti, G., Frigerio, F., Coda, A., Antolini, L., ... Ascenzi, P. (1990). X-ray crystal structure of the bovine alpha-chymotrypsin/eglin c complex at 2.6 A resolution. Journal of molecular recognition : JMR, 3(4), 163-168.

X-ray crystal structure of the bovine alpha-chymotrypsin/eglin c complex at 2.6 A resolution. / Bolognesi, M.; Pugliese, L.; Gatti, G.; Frigerio, F.; Coda, A.; Antolini, L.; Schnebli, H. P.; Menegatti, E.; Amiconi, G.; Ascenzi, P.

In: Journal of molecular recognition : JMR, Vol. 3, No. 4, 08.1990, p. 163-168.

Research output: Contribution to journalArticle

Bolognesi, M, Pugliese, L, Gatti, G, Frigerio, F, Coda, A, Antolini, L, Schnebli, HP, Menegatti, E, Amiconi, G & Ascenzi, P 1990, 'X-ray crystal structure of the bovine alpha-chymotrypsin/eglin c complex at 2.6 A resolution.', Journal of molecular recognition : JMR, vol. 3, no. 4, pp. 163-168.
Bolognesi M, Pugliese L, Gatti G, Frigerio F, Coda A, Antolini L et al. X-ray crystal structure of the bovine alpha-chymotrypsin/eglin c complex at 2.6 A resolution. Journal of molecular recognition : JMR. 1990 Aug;3(4):163-168.
Bolognesi, M. ; Pugliese, L. ; Gatti, G. ; Frigerio, F. ; Coda, A. ; Antolini, L. ; Schnebli, H. P. ; Menegatti, E. ; Amiconi, G. ; Ascenzi, P. / X-ray crystal structure of the bovine alpha-chymotrypsin/eglin c complex at 2.6 A resolution. In: Journal of molecular recognition : JMR. 1990 ; Vol. 3, No. 4. pp. 163-168.
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abstract = "The crystal structure of the molecular complex formed by bovine alpha-chymotrypsin and the recombinant serine proteinase inhibitor eglin c from Hirudo medicinalis has been solved using monoclinic crystals of the complex, reported previously. Four circle diffractometer data at 3.0 A resolution were employed to determine the structure by molecular replacement techniques. Bovine alpha-chymotrypsin alone was used as the search model; it allowed us to correctly orient and translate the enzyme in the unit cell and to obtain sufficient electron density for positioning the eglin c molecule. After independent rigid body refinement of the two complex components, the molecular model yielded a crystallographic R factor of 0.39. Five iterative cycles of restrained crystallographic refinement and model building were conducted, gradually increasing resolution. The current R factor at 2.6 A resolution (diffractometer data) is 0.18. The model includes 56 solvent molecules. Eglin c binds to bovine alpha-chymotrypsin in a manner consistent with other known serine proteinase/inhibitor complex structures. The reactive site loop shows the expected conformation for productive binding and is in tight contact with bovine alpha-chymotrypsin between subsites P3 and P'2; Leu 451 acts as the P1 residue, located in the primary specificity S1 site of the enzyme. Hydrogen bonds equivalent to those observed in complexes of trypsin(ogen) with the pancreatic basic- and secretory-inhibitors are found around the scissile peptide bond.",
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AU - Frigerio, F.

AU - Coda, A.

AU - Antolini, L.

AU - Schnebli, H. P.

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