1ppe
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(New page: 200px<br /><applet load="1ppe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ppe, resolution 2.0Å" /> '''THE REFINED 2.0 ANGST...)
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Revision as of 21:52, 20 November 2007
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THE REFINED 2.0 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN BOVINE BETA-TRYPSIN AND CMTI-I, A TRYPSIN INHIBITOR FROM SQUASH SEEDS (CUCURBITA MAXIMA): TOPOLOGICAL SIMILARITY OF THE SQUASH SEED INHIBITORS WITH THE CARBOXYPEPTIDASE A INHIBITOR FROM POTATOES
Overview
The stoichiometric complex formed between bovine beta-trypsin and the, Cucurbita maxima trypsin inhibitor I (CMTI-I) was crystallized and its, X-ray crystal structure determined using Patterson search techniques. Its, structure has been crystallographically refined to a final R value of, 0.152 (6.0-2.0 A). CMTI-I is of ellipsoidal shape; it lacks helices or, beta-sheets, but consists of turns and connecting short polypeptide, stretches. The disulfide pairing is CYS-3I-20I, Cys-10I-22I and, Cys-16I-28I. According to the polypeptide fold and disulfide connectivity, its structure resembles that of the carboxypeptidase A inhibitor from, potatoes. Thirteen of the 29 inhibitor residues are in direct contact with, trypsin; most of them are in the primary binding segment Val-2I, (P4)-Glu-9I (P4') which contains the reactive site bond Arg-5I-Ile-6I and, is in a conformation observed also for other serine proteinase inhibitors.
About this Structure
1PPE is a Protein complex structure of sequences from Bos taurus. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes., Bode W, Greyling HJ, Huber R, Otlewski J, Wilusz T, FEBS Lett. 1989 Jan 2;242(2):285-92. PMID:2914611
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