1m1d: Difference between revisions

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==TETRAHYMENA GCN5 WITH BOUND BISUBSTRATE ANALOG INHIBITOR==
==TETRAHYMENA GCN5 WITH BOUND BISUBSTRATE ANALOG INHIBITOR==
<StructureSection load='1m1d' size='340' side='right' caption='[[1m1d]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1m1d' size='340' side='right'caption='[[1m1d]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1m1d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Tetth Tetth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M1D FirstGlance]. <br>
<table><tr><td colspan='2'>[[1m1d]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M1D FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LYX:N-(2-COENZYME+A)-PROPANOYL-LYSINE'>LYX</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]] 2.2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qsn|1qsn]], [[1qsr|1qsr]], [[1qst|1qst]], [[1ygh|1ygh]], [[1cmo|1cmo]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LYX:N-(2-COENZYME+A)-PROPANOYL-LYSINE'>LYX</scene></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=1m1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1d OCA], [http://pdbe.org/1m1d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m1d RCSB], [http://www.ebi.ac.uk/pdbsum/1m1d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m1d ProSAT]</span></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=1m1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1d OCA], [https://pdbe.org/1m1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m1d RCSB], [https://www.ebi.ac.uk/pdbsum/1m1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m1d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H3_YEAST H3_YEAST]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m1/1m1d_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m1/1m1d_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 18: Line 20:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m1d ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m1d ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Histone acetyltransferases (HATs) use acetyl CoA to acetylate target lysine residues within histones and other transcription factors, such as the p53 tumor suppressor, to promote gene activation. HAT enzymes fall into subfamilies with divergence in sequence and substrate preference. Several HAT proteins have been implicated in human cancer. We have previously reported on the preparation of peptide-CoA conjugate inhibitors with distinct specificities for the p300/CBP [cAMP response element binding protein (CREB)-binding protein] or GCN5 HAT subfamilies. Here we report on the crystal structure of the GCN5 HAT bound to a peptide-CoA conjugate containing CoA covalently attached through an isopropionyl linker to Lys-14 of a 20-aa N-terminal fragment of histone H3. Surprisingly, the structure reveals that the H3 portion of the inhibitor is bound outside of the binding site for the histone substrate and that only five of the 20 aa residues of the inhibitor are ordered. Rearrangements within the C-terminal region of the GCN5 protein appear to mediate this peptide displacement. Mutational and enzymatic data support the hypothesis that the observed structure corresponds to a late catalytic intermediate. The structure also provides a structural scaffold for the design of HAT-specific inhibitors that may have therapeutic applications for the treatment of HAT-mediated cancers.
Structure of the GCN5 histone acetyltransferase bound to a bisubstrate inhibitor.,Poux AN, Cebrat M, Kim CM, Cole PA, Marmorstein R Proc Natl Acad Sci U S A. 2002 Oct 29;99(22):14065-70. Epub 2002 Oct 21. PMID:12391296<ref>PMID:12391296</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1m1d" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Tetth]]
[[Category: Large Structures]]
[[Category: Cebrat, M]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Cole, P A]]
[[Category: Tetrahymena thermophila]]
[[Category: Kim, C M]]
[[Category: Cebrat M]]
[[Category: Marmorstein, R]]
[[Category: Cole PA]]
[[Category: Poux, A N]]
[[Category: Kim CM]]
[[Category: Gcn5-related n-acetyltransferase]]
[[Category: Marmorstein R]]
[[Category: Histone acetyltransferase]]
[[Category: Poux AN]]
[[Category: Inhibitor complex]]
[[Category: Transcription factor]]
[[Category: Transferase]]

Latest revision as of 11:30, 10 April 2024

TETRAHYMENA GCN5 WITH BOUND BISUBSTRATE ANALOG INHIBITORTETRAHYMENA GCN5 WITH BOUND BISUBSTRATE ANALOG INHIBITOR

Structural highlights

1m1d is a 4 chain structure with sequence from Saccharomyces cerevisiae and Tetrahymena thermophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

H3_YEAST

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1m1d, resolution 2.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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