2ndg

From Proteopedia

(Difference between revisions)

Revision as of 21:00, 10 September 2016

Solution NMR structures of AF9 yeats domain in complex with histone H3 crotonylation at K18

Structural highlights

2ndg is a 2 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	2ndf
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[AF9_HUMAN] A chromosomal aberration involving MLLT3 is associated with acute leukemias. Translocation t(9;11)(p22;q23) with KMT2A/MLL1. The result is a rogue activator protein.

Function

[AF9_HUMAN] Component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA.^[1] ^[2]

Publication Abstract from PubMed

Histone lysine acylations play an important role in the regulation of gene transcription in chromatin. Unlike histone acetyl-lysine, molecular recognition of a recently identified crotonyl-lysine mark is much less understood. Here, we report that the YEATS domain of AF9 preferentially binds crotonyl-lysine over acetyl-lysine in histone H3. Nuclear magnetic resonance structural analysis reveals that crotonyl-lysine of histone H3 lysine 18 is engulfed deep in an aromatic cage of the YEATS domain where the carbonyl oxygen of crotonyl-lysine forms a hydrogen bond with the backbone amide of protein residue Tyr78. The crotonyl-lysine, through its unique electron-rich double-bond side chain, engages pi-pi aromatic stacking and extended hydrophobic/aromatic interactions with the YEATS domain compared with acetyl-lysine. Our mutational analysis confirmed key protein residues Phe59 and Tyr78 for crotonyl-lysine recognition. Importantly, our findings present a new structural mechanism of protein-protein interactions mediated by histone lysine crotonylation, and show how the cells interpret acyl-lysine marks in different biological contexts.

Structural Insights into Histone Crotonyl-Lysine Recognition by the AF9 YEATS Domain.,Zhang Q, Zeng L, Zhao C, Ju Y, Konuma T, Zhou MM Structure. 2016 Sep 6;24(9):1606-1612. doi: 10.1016/j.str.2016.05.023. Epub 2016 , Aug 18. PMID:27545619^[3]

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

References

↑ Lin C, Smith ER, Takahashi H, Lai KC, Martin-Brown S, Florens L, Washburn MP, Conaway JW, Conaway RC, Shilatifard A. AFF4, a component of the ELL/P-TEFb elongation complex and a shared subunit of MLL chimeras, can link transcription elongation to leukemia. Mol Cell. 2010 Feb 12;37(3):429-37. doi: 10.1016/j.molcel.2010.01.026. PMID:20159561 doi:10.1016/j.molcel.2010.01.026
↑ He N, Liu M, Hsu J, Xue Y, Chou S, Burlingame A, Krogan NJ, Alber T, Zhou Q. HIV-1 Tat and host AFF4 recruit two transcription elongation factors into a bifunctional complex for coordinated activation of HIV-1 transcription. Mol Cell. 2010 May 14;38(3):428-38. doi: 10.1016/j.molcel.2010.04.013. PMID:20471948 doi:10.1016/j.molcel.2010.04.013
↑ Zhang Q, Zeng L, Zhao C, Ju Y, Konuma T, Zhou MM. Structural Insights into Histone Crotonyl-Lysine Recognition by the AF9 YEATS Domain. Structure. 2016 Sep 6;24(9):1606-1612. doi: 10.1016/j.str.2016.05.023. Epub 2016 , Aug 18. PMID:27545619 doi:http://dx.doi.org/10.1016/j.str.2016.05.023

1 Structural highlights
2 Disease
3 Function
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/2ndg"

Categories: Zeng, L | Zhou, M | Crotonylation | Histone | Transcription

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2ndg is ON HOLD
+==Solution NMR structures of AF9 yeats domain in complex with histone H3 crotonylation at K18==
+<StructureSection load='2ndg' size='340' side='right' caption='[[2ndg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2ndg]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NDG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NDG FirstGlance]. <br>
+</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCR:N-6-CROTONYL-L-LYSINE'>KCR</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ndf|2ndf]]</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=2ndg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ndg OCA], [http://pdbe.org/2ndg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ndg RCSB], [http://www.ebi.ac.uk/pdbsum/2ndg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ndg ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/AF9_HUMAN AF9_HUMAN]] A chromosomal aberration involving MLLT3 is associated with acute leukemias. Translocation t(9;11)(p22;q23) with KMT2A/MLL1. The result is a rogue activator protein.
+== Function ==
+[[http://www.uniprot.org/uniprot/AF9_HUMAN AF9_HUMAN]] Component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA.<ref>PMID:20159561</ref> <ref>PMID:20471948</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Histone lysine acylations play an important role in the regulation of gene transcription in chromatin. Unlike histone acetyl-lysine, molecular recognition of a recently identified crotonyl-lysine mark is much less understood. Here, we report that the YEATS domain of AF9 preferentially binds crotonyl-lysine over acetyl-lysine in histone H3. Nuclear magnetic resonance structural analysis reveals that crotonyl-lysine of histone H3 lysine 18 is engulfed deep in an aromatic cage of the YEATS domain where the carbonyl oxygen of crotonyl-lysine forms a hydrogen bond with the backbone amide of protein residue Tyr78. The crotonyl-lysine, through its unique electron-rich double-bond side chain, engages pi-pi aromatic stacking and extended hydrophobic/aromatic interactions with the YEATS domain compared with acetyl-lysine. Our mutational analysis confirmed key protein residues Phe59 and Tyr78 for crotonyl-lysine recognition. Importantly, our findings present a new structural mechanism of protein-protein interactions mediated by histone lysine crotonylation, and show how the cells interpret acyl-lysine marks in different biological contexts.
-Authors: Zeng, L., Zhou, M.
+Structural Insights into Histone Crotonyl-Lysine Recognition by the AF9 YEATS Domain.,Zhang Q, Zeng L, Zhao C, Ju Y, Konuma T, Zhou MM Structure. 2016 Sep 6;24(9):1606-1612. doi: 10.1016/j.str.2016.05.023. Epub 2016 , Aug 18. PMID:27545619<ref>PMID:27545619</ref>
-Description: Solution NMR structures of AF9 yeats domain in complex with histone H3 crotonylation at K18
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Zhou, M]]
+<div class="pdbe-citations 2ndg" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Zeng, L]]
+[[Category: Zhou, M]]
+[[Category: Crotonylation]]
+[[Category: Histone]]
+[[Category: Transcription]]

2ndg

From Proteopedia

Revision as of 21:00, 10 September 2016

Solution NMR structures of AF9 yeats domain in complex with histone H3 crotonylation at K18

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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