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.


6r0n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:12, 24 January 2024) (edit) (undo)
 
Line 1: Line 1:
-
====
+
==Histone fold domain of AtNF-YB2/NF-YC3 in I2==
-
<StructureSection load='6r0n' size='340' side='right'caption='[[6r0n]]' scene=''>
+
<StructureSection load='6r0n' size='340' side='right'caption='[[6r0n]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6r0n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R0N FirstGlance]. <br>
-
</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=6r0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r0n OCA], [https://pdbe.org/6r0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r0n RCSB], [https://www.ebi.ac.uk/pdbsum/6r0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r0n ProSAT]</span></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]] 2.1&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6r0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r0n OCA], [https://pdbe.org/6r0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r0n RCSB], [https://www.ebi.ac.uk/pdbsum/6r0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r0n ProSAT]</span></td></tr>
</table>
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/NFYB2_ARATH NFYB2_ARATH] Component of the NF-Y/HAP transcription factor complex (By similarity). The NF-Y complex stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters (By similarity).[UniProtKB:Q84W66]
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
NF-Y transcription factor comprises three subunits: NF-YA, NF-YB and NF-YC. NF-YB and NF-YC dimerize through their histone fold domain (HFD), which can bind DNA in a non-sequence-specific fashion while serving as a scaffold for NF-YA trimerization. Upon trimerization, NF-YA specifically recognizes the CCAAT box sequence on promoters and enhancers. In plants, each NF-Y subunit is encoded by several genes giving rise to hundreds of potential heterotrimeric combinations. In addition, plant NF-YBs and NF-YCs interact with other protein partners to recognize a plethora of genomic motifs, as the CCT protein family that binds CORE sites. The NF-Y subunit organization and its DNA-binding properties, together with the NF-Y HFD capacity to adapt different protein modules, represent plant-specific features that play a key role in development, growth and reproduction. Despite their relevance, these features are still poorly understood at the molecular level. Here, we present the structures of Arabidopsis and rice NF-YB/NF-YC dimers, and of an Arabidopsis NF-Y trimer in complex with the FT CCAAT box, together with biochemical data on NF-Y mutants. The dimeric structures identify the key residues for NF-Y HFD stabilization. The NF-Y/DNA structure and the mutation experiments shed light on HFD trimerization interface properties and the NF-YA sequence appetite for the bases flanking the CCAAT motif. These data explain the logic of plant NF-Y gene expansion: the trimerization adaptability and the flexible DNA-binding rules serve the scopes of accommodating the large number of NF-YAs, CCTs and possibly other NF-Y HFD binding partners and a diverse audience of genomic motifs.
 +
 +
Structural determinants for NF-Y subunit organization and NF-Y/DNA association in plants.,Chaves-Sanjuan A, Gnesutta N, Gobbini A, Martignago D, Bernardini A, Fornara F, Mantovani R, Nardini M Plant J. 2021 Jan;105(1):49-61. doi: 10.1111/tpj.15038. Epub 2020 Nov 27. PMID:33098724<ref>PMID:33098724</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 6r0n" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Nuclear transcription factor Y|Nuclear transcription factor Y]]
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Z-disk]]
+
[[Category: Bernardini A]]
 +
[[Category: Chaves-Sanjuan A]]
 +
[[Category: Fornara F]]
 +
[[Category: Gnesutta N]]
 +
[[Category: Mantovani R]]
 +
[[Category: Nardini M]]

Current revision

Histone fold domain of AtNF-YB2/NF-YC3 in I2

PDB ID 6r0n

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools