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Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.9 A resolution.
Acta Crystallogr D Biol Crystallogr. 1999 Jan; 55(Pt 1):25-30.AC

Abstract

The crystal structure of a bifunctional inhibitor of alpha-amylase and trypsin from the seeds of ragi (Indian finger millet, Eleusine coracana Gaertneri) has been determined by an X-ray diffraction method. The inhibitor consists of 122 amino acids with five disulfide bridges and belongs to the plant alpha-amylase/trypsin-inhibitor family. This is the first crystal structure determination of a member of this family. The protein, purified from the seeds of ragi, has a molecular mass of 13300 Da with a pI of 10.3. Crystals were grown by a microdialysis method using ammonium sulfate as precipitant. The improved purification protocol and the modified crystallization conditions enabled reproducible growth of the crystals. The cell parameters are a = 41. 2, b = 47.4, c = 55.9 A. The intensity data were collected to 2.9 A resolution, and the crystal structure was determined using the molecular-replacement method. The structure was refined using the X-PLOR and CCP4 program packages to a conventional R factor of 21%. The structure contains four alpha-helices between residues 19-29, 37-51, 56-65 and 90-95, and two short antiparallel beta-strands between residues 67-70 and 73-75.

Authors+Show Affiliations

Department of Biophysics, All India Institute of Medical Sciences, New Delhi 110029, India.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10089391

Citation

Gourinath, S, et al. "Structure of the Bifunctional Inhibitor of Trypsin and Alpha-amylase From Ragi Seeds at 2.9 a Resolution." Acta Crystallographica. Section D, Biological Crystallography, vol. 55, no. Pt 1, 1999, pp. 25-30.
Gourinath S, Srinivasan A, Singh TP. Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.9 A resolution. Acta Crystallogr D Biol Crystallogr. 1999;55(Pt 1):25-30.
Gourinath, S., Srinivasan, A., & Singh, T. P. (1999). Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.9 A resolution. Acta Crystallographica. Section D, Biological Crystallography, 55(Pt 1), 25-30.
Gourinath S, Srinivasan A, Singh TP. Structure of the Bifunctional Inhibitor of Trypsin and Alpha-amylase From Ragi Seeds at 2.9 a Resolution. Acta Crystallogr D Biol Crystallogr. 1999;55(Pt 1):25-30. PubMed PMID: 10089391.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.9 A resolution. AU - Gourinath,S, AU - Srinivasan,A, AU - Singh,T P, Y1 - 1999/01/01/ PY - 1998/02/27/received PY - 1998/04/30/accepted PY - 1999/3/25/pubmed PY - 2000/6/23/medline PY - 1999/3/25/entrez SP - 25 EP - 30 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 55 IS - Pt 1 N2 - The crystal structure of a bifunctional inhibitor of alpha-amylase and trypsin from the seeds of ragi (Indian finger millet, Eleusine coracana Gaertneri) has been determined by an X-ray diffraction method. The inhibitor consists of 122 amino acids with five disulfide bridges and belongs to the plant alpha-amylase/trypsin-inhibitor family. This is the first crystal structure determination of a member of this family. The protein, purified from the seeds of ragi, has a molecular mass of 13300 Da with a pI of 10.3. Crystals were grown by a microdialysis method using ammonium sulfate as precipitant. The improved purification protocol and the modified crystallization conditions enabled reproducible growth of the crystals. The cell parameters are a = 41. 2, b = 47.4, c = 55.9 A. The intensity data were collected to 2.9 A resolution, and the crystal structure was determined using the molecular-replacement method. The structure was refined using the X-PLOR and CCP4 program packages to a conventional R factor of 21%. The structure contains four alpha-helices between residues 19-29, 37-51, 56-65 and 90-95, and two short antiparallel beta-strands between residues 67-70 and 73-75. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/10089391/Structure_of_the_bifunctional_inhibitor_of_trypsin_and_alpha_amylase_from_ragi_seeds_at_2_9_A_resolution_ L2 - http://scripts.iucr.org/cgi-bin/paper?S0907444998006271 DB - PRIME DP - Unbound Medicine ER -