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==Structure of Bromodomain from human BAZ1A==
==Structure of Bromodomain from human BAZ1A==
<StructureSection load='5uiy' size='340' side='right' caption='[[5uiy]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
<StructureSection load='5uiy' size='340' side='right'caption='[[5uiy]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5uiy]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UIY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UIY FirstGlance]. <br>
<table><tr><td colspan='2'>[[5uiy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UIY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UIY FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</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]] 1.687&#8491;</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=5uiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uiy OCA], [http://pdbe.org/5uiy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uiy RCSB], [http://www.ebi.ac.uk/pdbsum/5uiy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uiy ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</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=5uiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uiy OCA], [https://pdbe.org/5uiy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uiy RCSB], [https://www.ebi.ac.uk/pdbsum/5uiy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uiy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/BAZ1A_HUMAN BAZ1A_HUMAN]] Component of the ACF complex, an ATP-dependent chromatin remodeling complex, that regulates spacing of nucleosomes using ATP to generate evenly spaced nucleosomes along the chromatin. The ATPase activity of the complex is regulated by the length of flanking DNA. Also involved in facilitating the DNA replication process. BAZ1A is the accessory, non-catalytic subunit of the complex which can enhance and direct the process provided by the ATPase subunit, SMARCA5, probably through targeting pericentromeric heterochromatin in late S phase. Moves end-positioned nucleosomes to a predominantly central position. May have a role in nuclear receptor-mediated transcription repression.  Component of the histone-fold protein complex CHRAC complex which faciliates nucleosome sliding by the ACF complex and enhances ACF-mediated chromatin assembly. The C-terminal regions of both CHRAC1 and POLE1 are required for these functions.  
[https://www.uniprot.org/uniprot/BAZ1A_HUMAN BAZ1A_HUMAN] Component of the ACF complex, an ATP-dependent chromatin remodeling complex, that regulates spacing of nucleosomes using ATP to generate evenly spaced nucleosomes along the chromatin. The ATPase activity of the complex is regulated by the length of flanking DNA. Also involved in facilitating the DNA replication process. BAZ1A is the accessory, non-catalytic subunit of the complex which can enhance and direct the process provided by the ATPase subunit, SMARCA5, probably through targeting pericentromeric heterochromatin in late S phase. Moves end-positioned nucleosomes to a predominantly central position. May have a role in nuclear receptor-mediated transcription repression.  Component of the histone-fold protein complex CHRAC complex which faciliates nucleosome sliding by the ACF complex and enhances ACF-mediated chromatin assembly. The C-terminal regions of both CHRAC1 and POLE1 are required for these functions.
 
==See Also==
*[[Bromodomain adjacent to zinc finger|Bromodomain adjacent to zinc finger]]
*[[Bromodomain adjacent to zinc finger 3D structures|Bromodomain adjacent to zinc finger 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Oppikofer, M]]
[[Category: Homo sapiens]]
[[Category: Sudhamsu, J]]
[[Category: Large Structures]]
[[Category: Acf]]
[[Category: Oppikofer M]]
[[Category: Baz1a]]
[[Category: Sudhamsu J]]
[[Category: Bromodomain]]
[[Category: Dna-damage]]
[[Category: Transcription]]

Latest revision as of 17:27, 6 March 2024

Structure of Bromodomain from human BAZ1AStructure of Bromodomain from human BAZ1A

Structural highlights

5uiy is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.687Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BAZ1A_HUMAN Component of the ACF complex, an ATP-dependent chromatin remodeling complex, that regulates spacing of nucleosomes using ATP to generate evenly spaced nucleosomes along the chromatin. The ATPase activity of the complex is regulated by the length of flanking DNA. Also involved in facilitating the DNA replication process. BAZ1A is the accessory, non-catalytic subunit of the complex which can enhance and direct the process provided by the ATPase subunit, SMARCA5, probably through targeting pericentromeric heterochromatin in late S phase. Moves end-positioned nucleosomes to a predominantly central position. May have a role in nuclear receptor-mediated transcription repression. Component of the histone-fold protein complex CHRAC complex which faciliates nucleosome sliding by the ACF complex and enhances ACF-mediated chromatin assembly. The C-terminal regions of both CHRAC1 and POLE1 are required for these functions.

See Also

5uiy, resolution 1.69Å

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