This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1nar
From Proteopedia
|
CRYSTAL STRUCTURE OF NARBONIN REFINED AT 1.8 ANGSTROMS RESOLUTION
Overview
The three-dimensional structure of narbonin, a seed protein from Vicia, narbonensis L, has been determined at 1.8 A resolution. Phase information, was obtained by multiple isomorphous replacement and optimized anomalous, dispersion. The narbonin structure was initially traced with only 17%, amino-acid sequence information and preliminarily refined to a, crystallographic R-factor of 16.5%. It is now refined to 15.9% using full, sequence information derived from cDNA and after the addition of more, solvent molecules. The monomeric molecule of narbonin is an eight-stranded, parallel beta-barrel surrounded by alpha-helices in a beta/alpha-topology, similar to that first observed in triose phosphate isomerase. Differences, exist in the N-terminal part of the polypeptide chain, where the first, helix is replaced by a loop and the second beta-strand is followed by an, additional antiparallel alpha-sheet placed parallel on top of, alpha-helices alpha3 and alpha4. Two short additional secondary structures, are present. The first, an alpha-helix, is situated between the seventh, beta-strand and the following helix, and the second, which is a 3(10), helix, between the eighth strand and the C-terminal helix. The most, striking observation is the lack of a known enzymatic function for, narbonin, because all TIM-like structures known so far are enzymes.
About this Structure
1NAR is a Single protein structure of sequence from Vicia narbonensis. Full crystallographic information is available from OCA.
Reference
Crystal structure of narbonin at 1.8 A resolution., Hennig M, Pfeffer-Hennig S, Dauter Z, Wilson KS, Schlesier B, Nong VH, Acta Crystallogr D Biol Crystallogr. 1995 Mar 1;51(Pt 2):177-89. PMID:15299319
Page seeded by OCA on Sat Nov 24 22:51:19 2007
