2zgg

From Proteopedia

(Difference between revisions)

Current revision

Asn-hydroxylation stabilises the ankyrin repeat domain fold

Structural highlights

2zgg is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

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

Publication Abstract from PubMed

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.

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^[1]

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

References

↑ Kelly L, McDonough MA, Coleman ML, Ratcliffe PJ, Schofield CJ. Asparagine beta-hydroxylation stabilizes the ankyrin repeat domain fold. Mol Biosyst. 2009 Jan;5(1):52-8. Epub 2008 Oct 29. PMID:19081931 doi:10.1039/b815271c

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2zgg"

Categories: Large Structures | McDonough MA | Schofield CJ

@@ Line 1: / Line 1: @@
 ==Asn-hydroxylation stabilises the ankyrin repeat domain fold==
-<StructureSection load='2zgg' size='340' side='right' caption='[[2zgg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='2zgg' size='340' side='right'caption='[[2zgg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2zgg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZGG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZGG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2zgg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZGG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZGG FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</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&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zgd|2zgd]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</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=2zgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zgg OCA], [http://pdbe.org/2zgg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zgg RCSB], [http://www.ebi.ac.uk/pdbsum/2zgg PDBsum]</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=2zgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zgg OCA], [https://pdbe.org/2zgg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zgg RCSB], [https://www.ebi.ac.uk/pdbsum/2zgg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zgg ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 11: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zg/2zgg_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zg/2zgg_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 31: @@
 __TOC__
 </StructureSection>
-[[Category: McDonough, M A]]
+[[Category: Large Structures]]
-[[Category: Schofield, C J]]
+[[Category: McDonough MA]]
-[[Category: Ankyrin repeat]]
+[[Category: Schofield CJ]]
-[[Category: De novo protein]]
-[[Category: Unhydroxylated]]

2zgg

From Proteopedia

Current revision

Asn-hydroxylation stabilises the ankyrin repeat domain fold

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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