1nar
From Proteopedia
(New page: 200px<br /><applet load="1nar" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nar, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1nar.gif|left|200px]]<br /><applet load="1nar" size=" | + | [[Image:1nar.gif|left|200px]]<br /><applet load="1nar" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nar, resolution 1.8Å" /> | caption="1nar, resolution 1.8Å" /> | ||
'''CRYSTAL STRUCTURE OF NARBONIN REFINED AT 1.8 ANGSTROMS RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF NARBONIN REFINED AT 1.8 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of narbonin, a seed protein from Vicia | + | 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== | ==About this Structure== | ||
| - | 1NAR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vicia_narbonensis Vicia narbonensis]. Full crystallographic information is available from [http:// | + | 1NAR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vicia_narbonensis Vicia narbonensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NAR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Hennig, M.]] | [[Category: Hennig, M.]] | ||
[[Category: Schlesier, B.]] | [[Category: Schlesier, B.]] | ||
| - | [[Category: Wilson, K | + | [[Category: Wilson, K S.]] |
[[Category: plant seed protein]] | [[Category: plant seed protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:04 2008'' |
Revision as of 12:04, 21 February 2008
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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
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