2zgd

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[[Image:2zgd.jpg|left|200px]]
 
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{{Structure
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==Asn-hydroxylation stabilises the ankyrin repeat domain fold==
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|PDB= 2zgd |SIZE=350|CAPTION= <scene name='initialview01'>2zgd</scene>, resolution 1.900&Aring;
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<StructureSection load='2zgd' size='340' side='right'caption='[[2zgd]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Cd+Binding+Site+For+Residue+A+410'>AC1</scene>, <scene name='pdbsite=AC2:Cd+Binding+Site+For+Residue+A+411'>AC2</scene>, <scene name='pdbsite=AC3:Cd+Binding+Site+For+Residue+A+412'>AC3</scene>, <scene name='pdbsite=AC4:Cd+Binding+Site+For+Residue+A+413'>AC4</scene>, <scene name='pdbsite=AC5:Cd+Binding+Site+For+Residue+A+414'>AC5</scene>, <scene name='pdbsite=AC6:Cl+Binding+Site+For+Residue+A+415'>AC6</scene> and <scene name='pdbsite=AC7:Cl+Binding+Site+For+Residue+A+416'>AC7</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=AHB:BETA-HYDROXYASPARAGINE'>AHB</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
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<table><tr><td colspan='2'>[[2zgd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZGD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZGD FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AHB:BETA-HYDROXYASPARAGINE'>AHB</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zgd OCA], [https://pdbe.org/2zgd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zgd RCSB], [https://www.ebi.ac.uk/pdbsum/2zgd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zgd ProSAT]</span></td></tr>
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|RELATEDENTRY=[[2zgg|2ZGG]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zgd OCA], [http://www.ebi.ac.uk/pdbsum/2zgd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2zgd RCSB]</span>
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== Evolutionary Conservation ==
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}}
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zg/2zgd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2zgd ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ankyrin repeats (ARs) are one of the most common structural motifs among eukaryotic proteins. Recent analyses have shown that factor inhibiting hypoxia-inducible factor (FIH) catalyses the hydroxylation of highly conserved Asn-residues within ankyrin repeat domains (ARDs). However, the effect of Asn-hydroxylation on ARD structure is unknown. Supporting the proposal that FIH-mediated ARD hydroxylation is ubiquitous we report that consensus ARD proteins are FIH substrates both in vitro and in vivo. X-ray diffraction analyses revealed that hydroxylation does not alter the archetypical ARD conformation in the crystalline state. However, other biophysical analyses revealed that hydroxylation significantly stabilizes the ARD fold in solution. We propose that intracellular protein hydroxylation is much more common than previously thought and that one of its roles is stabilization of localized regions of ARD folds.
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'''Asn-hydroxylation stabilises the ankyrin repeat domain fold'''
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Asparagine beta-hydroxylation stabilizes the ankyrin repeat domain fold.,Kelly L, McDonough MA, Coleman ML, Ratcliffe PJ, Schofield CJ Mol Biosyst. 2009 Jan;5(1):52-8. Epub 2008 Oct 29. PMID:19081931<ref>PMID:19081931</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==Overview==
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</div>
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The stability and activity of hypoxia-inducible factor (HIF) are regulated by the post-translational hydroxylation of specific prolyl and asparaginyl residues. We show that the HIF asparaginyl hydroxylase, factor inhibiting HIF (FIH), also catalyzes hydroxylation of highly conserved asparaginyl residues within ankyrin repeat (AR) domains (ARDs) of endogenous Notch receptors. AR hydroxylation decreases the extent of ARD binding to FIH while not affecting signaling through the canonical Notch pathway. ARD proteins were found to efficiently compete with HIF for FIH-dependent hydroxylation. Crystallographic analyses of the hydroxylated Notch ARD (2.35A) and of Notch peptides bound to FIH (2.4-2.6A) reveal the stereochemistry of hydroxylation on the AR and imply that significant conformational changes are required in the ARD fold in order to enable hydroxylation at the FIH active site. We propose that ARD proteins function as natural inhibitors of FIH and that the hydroxylation status of these proteins provides another oxygen-dependent interface that modulates HIF signaling.
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<div class="pdbe-citations 2zgd" style="background-color:#fffaf0;"></div>
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== References ==
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==About this Structure==
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<references/>
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2ZGD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZGD OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor., Coleman ML, McDonough MA, Hewitson KS, Coles C, Mecinovic J, Edelmann M, Cook KM, Cockman ME, Lancaster DE, Kessler BM, Oldham NJ, Ratcliffe PJ, Schofield CJ, J Biol Chem. 2007 Aug 17;282(33):24027-38. Epub 2007 Jun 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17573339 17573339]
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[[Category: McDonough MA]]
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[[Category: Single protein]]
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[[Category: Schofield CJ]]
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[[Category: McDonough, M A.]]
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[[Category: Schofield, C J.]]
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[[Category: ankyrin repeat]]
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[[Category: de novo protein]]
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[[Category: hydroxylated]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:20:58 2008''
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Current revision

Asn-hydroxylation stabilises the ankyrin repeat domain fold

PDB ID 2zgd

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