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==Crystal structure of the chromatin factor RCC1 in complex with the nucleosome core particle==
==Crystal structure of the chromatin factor RCC1 in complex with the nucleosome core particle==
<StructureSection load='3mvd' size='340' side='right' caption='[[3mvd]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='3mvd' size='340' side='right'caption='[[3mvd]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3mvd]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog] and [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MVD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MVD FirstGlance]. <br>
<table><tr><td colspan='2'>[[3mvd]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MVD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MVD FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kx5|1kx5]], [[1zla|1zla]]</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]] 2.9&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HISTONE H3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), HISTONE H4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), LOC494591 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), HISTONE H2B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), Bj1, CG10480, RCC1 (Bj1) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=3mvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mvd OCA], [https://pdbe.org/3mvd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mvd RCSB], [https://www.ebi.ac.uk/pdbsum/3mvd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mvd ProSAT]</span></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=3mvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mvd OCA], [http://pdbe.org/3mvd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mvd RCSB], [http://www.ebi.ac.uk/pdbsum/3mvd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mvd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/H2B11_XENLA H2B11_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/H32_XENLA H32_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/RCC1_DROME RCC1_DROME]] Promotes the exchange of Ran-bound GDP by GTP. Involved in the regulation of onset of chromosome condensation in the S phase. Binds to chromatin.<ref>PMID:2022190</ref>  [[http://www.uniprot.org/uniprot/H4_XENLA H4_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
[https://www.uniprot.org/uniprot/Q6AZJ8_XENLA Q6AZJ8_XENLA]  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Histone|Histone]]
*[[Histone 3D structures|Histone 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: African clawed frog]]
[[Category: Drosophila melanogaster]]
[[Category: Drome]]
[[Category: Large Structures]]
[[Category: England, J R]]
[[Category: Xenopus laevis]]
[[Category: Makde, R D]]
[[Category: England JR]]
[[Category: Tan, S]]
[[Category: Makde RD]]
[[Category: Yennawar, H P]]
[[Category: Tan S]]
[[Category: 7-bladed beta-propeller]]
[[Category: Yennawar HP]]
[[Category: Ncp-chromatin factor complex]]
[[Category: Protein-dna complex]]
[[Category: Signaling protein-structural protein-dna complex]]

Latest revision as of 12:02, 6 September 2023

Crystal structure of the chromatin factor RCC1 in complex with the nucleosome core particleCrystal structure of the chromatin factor RCC1 in complex with the nucleosome core particle

Structural highlights

3mvd is a 12 chain structure with sequence from Drosophila melanogaster and Xenopus laevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q6AZJ8_XENLA

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 small GTPase Ran enzyme regulates critical eukaryotic cellular functions including nuclear transport and mitosis through the creation of a RanGTP gradient around the chromosomes. This concentration gradient is created by the chromatin-bound RCC1 (regulator of chromosome condensation) protein, which recruits Ran to nucleosomes and activates Ran's nucleotide exchange activity. Although RCC1 has been shown to bind directly with the nucleosome, the molecular details of this interaction were not known. Here we determine the crystal structure of a complex of Drosophila RCC1 and the nucleosome core particle at 2.9 A resolution, providing an atomic view of how a chromatin protein interacts with the histone and DNA components of the nucleosome. Our structure also suggests that the Widom 601 DNA positioning sequence present in the nucleosomes forms a 145-base-pair nucleosome core particle, not the expected canonical 147-base-pair particle.

Structure of RCC1 chromatin factor bound to the nucleosome core particle.,Makde RD, England JR, Yennawar HP, Tan S Nature. 2010 Sep 30;467(7315):562-6. Epub 2010 Aug 25. PMID:20739938[1]

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

See Also

References

  1. ↑ Makde RD, England JR, Yennawar HP, Tan S. Structure of RCC1 chromatin factor bound to the nucleosome core particle. Nature. 2010 Sep 30;467(7315):562-6. Epub 2010 Aug 25. PMID:20739938 doi:10.1038/nature09321

3mvd, resolution 2.90Å

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