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.

1e0b

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Chromo shadow domain from fission yeast swi6 protein.

Structural highlights

1e0b is a 2 chain structure with sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SWI6_SCHPO Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Involved in the repression of the silent mating-type loci MAT2 and MAT3. May compact MAT2/3 into a heterochromatin-like conformation which represses the transcription of these silent cassettes.

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

BACKGROUND: Proteins such as HP1, found in fruit flies and mammals, and Swi6, its fission yeast homologue, carry a chromodomain (CD) and a chromo shadow domain (CSD). These proteins are required to form functional transcriptionally silent centromeric chromatin, and their mutation leads to chromosome segregation defects. CSDs have only been found in tandem in proteins containing the related CD. Most HP1-interacting proteins have been found to associate through the CSD and many of these ligands contain a conserved pentapeptide motif. RESULTS: The 1.9 A crystal structure of the Swi6 CSD is presented here. This reveals a novel dimeric structure that is distinct from the previously reported monomeric nuclear magnetic resonance (NMR) structure of the CD from the mouse modifier 1 protein (MoMOD1, also known as HP1beta or M31). A prominent pit with a non-polar base is generated at the dimer interface, and is commensurate with binding an extended pentapeptide motif. Sequence alignments based on this structure highlight differences between CDs and CSDs that are superimposed on a common structural core. The analyses also revealed a previously unrecognised circumferential hydrophobic sash around the surface of the CD structure. CONCLUSIONS: Dimerisation through the CSD of HP1-like proteins results in the simultaneous formation of a putative protein-protein interaction pit, providing a potential means of targeting CSD-containing proteins to particular chromatin sites.

Dimerisation of a chromo shadow domain and distinctions from the chromodomain as revealed by structural analysis.,Cowieson NP, Partridge JF, Allshire RC, McLaughlin PJ Curr Biol. 2000 May 4;10(9):517-25. PMID:10801440^[1]

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

References

↑ Cowieson NP, Partridge JF, Allshire RC, McLaughlin PJ. Dimerisation of a chromo shadow domain and distinctions from the chromodomain as revealed by structural analysis. Curr Biol. 2000 May 4;10(9):517-25. PMID:10801440

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e0b"

@@ Line 3: / Line 3: @@
 <StructureSection load='1e0b' size='340' side='right'caption='[[1e0b]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1e0b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0B OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1E0B FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1e0b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E0B FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PG:2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>1PG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1e0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0b OCA], [http://pdbe.org/1e0b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e0b RCSB], [http://www.ebi.ac.uk/pdbsum/1e0b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e0b ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PG:2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>1PG</scene></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=1e0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0b OCA], [https://pdbe.org/1e0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e0b RCSB], [https://www.ebi.ac.uk/pdbsum/1e0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e0b ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SWI6_SCHPO SWI6_SCHPO]] Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Involved in the repression of the silent mating-type loci MAT2 and MAT3. May compact MAT2/3 into a heterochromatin-like conformation which represses the transcription of these silent cassettes.
+[https://www.uniprot.org/uniprot/SWI6_SCHPO SWI6_SCHPO] Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Involved in the repression of the silent mating-type loci MAT2 and MAT3. May compact MAT2/3 into a heterochromatin-like conformation which represses the transcription of these silent cassettes.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Cbs 356]]
 [[Category: Large Structures]]
-[[Category: Allshire, R C]]
+[[Category: Schizosaccharomyces pombe]]
-[[Category: Cowieson, N P]]
+[[Category: Allshire RC]]
-[[Category: Mclaughlin, P J]]
+[[Category: Cowieson NP]]
-[[Category: Partridge, J F]]
+[[Category: Mclaughlin PJ]]
-[[Category: Chromatin-binding]]
+[[Category: Partridge JF]]
-[[Category: Chromodomain]]
-[[Category: Heterochromatin]]
-[[Category: Pombe]]
-[[Category: Shadow]]
-[[Category: Swi6]]

1e0b

From Proteopedia

Current revision

Chromo shadow domain from fission yeast swi6 protein.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox