1dvk

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(New page: 200px<br /><applet load="1dvk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dvk, resolution 2.15&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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'''CRYSTAL STRUCTURE OF THE FUNCTIONAL DOMAIN OF THE SPLICING FACTOR PRP18'''<br />
'''CRYSTAL STRUCTURE OF THE FUNCTIONAL DOMAIN OF THE SPLICING FACTOR PRP18'''<br />
==Overview==
==Overview==
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The splicing factor Prp18 is required for the second step of pre-mRNA, splicing. We have isolated and determined the crystal structure of a large, fragment of the Saccharomyces cerevisiae Prp18 that lacks the N-terminal, 79 amino acids. This fragment, called Prp18Delta79, is fully active in, yeast splicing in vitro and includes the sequences of Prp18 that have been, evolutionarily conserved. The core structure of Prp18Delta79 is compact, and globular, consisting of five alpha-helices that adopt a novel fold, that we have designated the five-helix X-bundle. The structure suggests, that one face of Prp18 interacts with the splicing factor Slu7, whereas, the more evolutionarily conserved amino acids in Prp18 form the opposite, face. The most highly conserved region of Prp18, a nearly invariant, stretch of 19 aa, forms part of a loop between two alpha-helices and may, interact with the U5 small nuclear ribonucleoprotein particles. The, structure is consistent with a model in which Prp18 forms a bridge between, Slu7 and the U5 small nuclear ribonucleoprotein particles.
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The splicing factor Prp18 is required for the second step of pre-mRNA splicing. We have isolated and determined the crystal structure of a large fragment of the Saccharomyces cerevisiae Prp18 that lacks the N-terminal 79 amino acids. This fragment, called Prp18Delta79, is fully active in yeast splicing in vitro and includes the sequences of Prp18 that have been evolutionarily conserved. The core structure of Prp18Delta79 is compact and globular, consisting of five alpha-helices that adopt a novel fold that we have designated the five-helix X-bundle. The structure suggests that one face of Prp18 interacts with the splicing factor Slu7, whereas the more evolutionarily conserved amino acids in Prp18 form the opposite face. The most highly conserved region of Prp18, a nearly invariant stretch of 19 aa, forms part of a loop between two alpha-helices and may interact with the U5 small nuclear ribonucleoprotein particles. The structure is consistent with a model in which Prp18 forms a bridge between Slu7 and the U5 small nuclear ribonucleoprotein particles.
==About this Structure==
==About this Structure==
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1DVK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DVK OCA].
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1DVK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DVK OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Horowitz, D.S.]]
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[[Category: Horowitz, D S.]]
[[Category: Jiang, J.]]
[[Category: Jiang, J.]]
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[[Category: Xu, R.M.]]
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[[Category: Xu, R M.]]
[[Category: crystal structure]]
[[Category: crystal structure]]
[[Category: pre-mrna splicing factor]]
[[Category: pre-mrna splicing factor]]
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[[Category: x-ray crystallography]]
[[Category: x-ray crystallography]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:37:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:55 2008''

Revision as of 10:20, 21 February 2008


1dvk, resolution 2.15Å

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CRYSTAL STRUCTURE OF THE FUNCTIONAL DOMAIN OF THE SPLICING FACTOR PRP18

Overview

The splicing factor Prp18 is required for the second step of pre-mRNA splicing. We have isolated and determined the crystal structure of a large fragment of the Saccharomyces cerevisiae Prp18 that lacks the N-terminal 79 amino acids. This fragment, called Prp18Delta79, is fully active in yeast splicing in vitro and includes the sequences of Prp18 that have been evolutionarily conserved. The core structure of Prp18Delta79 is compact and globular, consisting of five alpha-helices that adopt a novel fold that we have designated the five-helix X-bundle. The structure suggests that one face of Prp18 interacts with the splicing factor Slu7, whereas the more evolutionarily conserved amino acids in Prp18 form the opposite face. The most highly conserved region of Prp18, a nearly invariant stretch of 19 aa, forms part of a loop between two alpha-helices and may interact with the U5 small nuclear ribonucleoprotein particles. The structure is consistent with a model in which Prp18 forms a bridge between Slu7 and the U5 small nuclear ribonucleoprotein particles.

About this Structure

1DVK is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of the functional domain of the splicing factor Prp18., Jiang J, Horowitz DS, Xu RM, Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3022-7. PMID:10737784

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