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.

1dvk

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 18:36, 10 March 2021

CRYSTAL STRUCTURE OF THE FUNCTIONAL DOMAIN OF THE SPLICING FACTOR PRP18

Structural highlights

1dvk is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PRP18_YEAST] Component of the U4/U5/U6 snRNP, binding principally to the u5 snRNP. It is not absolutely required for the second step of pre-mRNA splicing at low temperatures but is required at higher temperatures. It may stabilize a particular conformation of the U5 snRNP or orient the U5 snRNP within the U4/U5/U6 snRNP or within the spliceosome.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dvk"

@@ Line 3: / Line 3: @@
 <StructureSection load='1dvk' size='340' side='right'caption='[[1dvk]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1dvk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DVK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1dvk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DVK FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dvk OCA], [http://pdbe.org/1dvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dvk RCSB], [http://www.ebi.ac.uk/pdbsum/1dvk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dvk ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dvk OCA], [https://pdbe.org/1dvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dvk RCSB], [https://www.ebi.ac.uk/pdbsum/1dvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dvk ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PRP18_YEAST PRP18_YEAST]] Component of the U4/U5/U6 snRNP, binding principally to the u5 snRNP. It is not absolutely required for the second step of pre-mRNA splicing at low temperatures but is required at higher temperatures. It may stabilize a particular conformation of the U5 snRNP or orient the U5 snRNP within the U4/U5/U6 snRNP or within the spliceosome.
+[[https://www.uniprot.org/uniprot/PRP18_YEAST PRP18_YEAST]] Component of the U4/U5/U6 snRNP, binding principally to the u5 snRNP. It is not absolutely required for the second step of pre-mRNA splicing at low temperatures but is required at higher temperatures. It may stabilize a particular conformation of the U5 snRNP or orient the U5 snRNP within the U4/U5/U6 snRNP or within the spliceosome.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 29: @@
 ==See Also==
-*[[Pre-mRNA-splicing factor|Pre-mRNA-splicing factor]]
+*[[Pre-mRNA splicing factors 3D structures|Pre-mRNA splicing factors 3D structures]]
 == References ==
 <references/>

1dvk

From Proteopedia

Revision as of 18:36, 10 March 2021

CRYSTAL STRUCTURE OF THE FUNCTIONAL DOMAIN OF THE SPLICING FACTOR PRP18

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox