5lou: Difference between revisions

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New page: '''Unreleased structure''' The entry 5lou is ON HOLD Authors: Carter, M., Stenmark, P. Description: human NUDT22 Category: Unreleased Structures Category: Stenmark, P [[Categor...
 
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'''Unreleased structure'''


The entry 5lou is ON HOLD
==human NUDT22==
<StructureSection load='5lou' size='340' side='right'caption='[[5lou]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lou]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LOU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=5lou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lou OCA], [https://pdbe.org/5lou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lou RCSB], [https://www.ebi.ac.uk/pdbsum/5lou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lou ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NUD22_HUMAN NUD22_HUMAN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human NUDT22 belongs to the diverse NUDIX family of proteins, but has, until now, remained uncharacterized. Here we show that human NUDT22 is a Mg(2+)-dependent UDP-glucose and UDP-galactose hydrolase, producing UMP and glucose 1-phosphate or galactose 1-phosphate. We present the structure of human NUDT22 alone and in a complex with the substrate UDP-glucose. These structures reveal a partially conserved NUDIX fold domain preceded by a unique N-terminal domain responsible for UDP moiety binding and recognition. The NUDIX domain of NUDT22 contains a modified NUDIX box identified using structural analysis and confirmed through functional analysis of mutants. Human NUDT22's distinct structure and function as a UDP-carbohydrate hydrolase establish a unique NUDIX protein subfamily.


Authors: Carter, M., Stenmark, P.
Human NUDT22 Is a UDP-Glucose/Galactose Hydrolase Exhibiting a Unique Structural Fold.,Carter M, Jemth AS, Carreras-Puigvert J, Herr P, Martinez Carranza M, Vallin KSA, Throup A, Helleday T, Stenmark P Structure. 2018 Feb 6;26(2):295-303.e6. doi: 10.1016/j.str.2018.01.004. PMID:29413322<ref>PMID:29413322</ref>


Description: human NUDT22
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Stenmark, P]]
<div class="pdbe-citations 5lou" style="background-color:#fffaf0;"></div>
[[Category: Carter, M]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Carter M]]
[[Category: Stenmark P]]