5xoo

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'''Unreleased structure'''
 
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The entry 5xoo is ON HOLD until Paper Publication
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==The structure of hydra Fam20 with sugar==
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<StructureSection load='5xoo' size='340' side='right'caption='[[5xoo]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5xoo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hydra_vulgaris Hydra vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XOO FirstGlance]. <br>
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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]] 2.85&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MBN:TOLUENE'>MBN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene></td></tr>
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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=5xoo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xoo OCA], [https://pdbe.org/5xoo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xoo RCSB], [https://www.ebi.ac.uk/pdbsum/5xoo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xoo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/T2MHS6_HYDVU T2MHS6_HYDVU]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Fam20 proteins are novel kinases that phosphorylate secreted proteins and proteoglycans. Fam20C phosphorylates hundreds of secreted proteins and is activated by the pseudokinase Fam20A. Fam20B phosphorylates a xylose residue to regulate proteoglycan synthesis. Despite these wide-ranging and important functions, the molecular and structural basis for the regulation and substrate specificity of these kinases are unknown. Here we report molecular characterizations of all three Fam20 kinases, and show that Fam20C is activated by the formation of an evolutionarily conserved homodimer or heterodimer with Fam20A. Fam20B has a unique active site for recognizing Galbeta1-4Xylbeta1, the initiator disaccharide within the tetrasaccharide linker region of proteoglycans. We further show that in animals the monomeric Fam20B preceded the appearance of the dimeric Fam20C, and the dimerization trait of Fam20C emerged concomitantly with a change in substrate specificity. Our results provide comprehensive structural, biochemical, and evolutionary insights into the function of the Fam20 kinases.
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Authors:
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Structure and evolution of the Fam20 kinases.,Zhang H, Zhu Q, Cui J, Wang Y, Chen MJ, Guo X, Tagliabracci VS, Dixon JE, Xiao J Nat Commun. 2018 Mar 23;9(1):1218. doi: 10.1038/s41467-018-03615-z. PMID:29572475<ref>PMID:29572475</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5xoo" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Hydra vulgaris]]
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[[Category: Large Structures]]
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[[Category: Xiao J]]
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[[Category: Zhang H]]

Current revision

The structure of hydra Fam20 with sugar

PDB ID 5xoo

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