1r3b: Difference between revisions
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<StructureSection load='1r3b' size='340' side='right'caption='[[1r3b]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1r3b' size='340' side='right'caption='[[1r3b]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1r3b]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1r3b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R3B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R3B FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MOB1 ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MOB1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r3b OCA], [https://pdbe.org/1r3b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r3b RCSB], [https://www.ebi.ac.uk/pdbsum/1r3b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r3b ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 09:28, 2 March 2022
Solution structure of xenopus laevis Mob1Solution structure of xenopus laevis Mob1
Structural highlights
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 PubMedProteins of the Mob1/phocein family are found in all eukaryotic cells. In yeast, they are activating subunits of Dbf2-related protein kinases involved in cell cycle control. Despite the wide occurrence of these proteins, their biological functions remain poorly understood. Here we report the solution structure of the Mob1 protein from Xenopus laevis solved by heteronuclear multidimensional NMR. The structure reveals a fold constituted by a central left-handed four-helix bundle, one connecting helix, two flanking helices and a long flexible loop. The clustering of two Cys and two His residues, and zinc measurement by atomic absorption spectroscopy support the existence of a zinc ion binding site. Our NMR structure is in good agreement with the recently described X-ray structure of human Mob1-A. Chemical shift perturbations observed upon addition of a peptide encompassing the basic region of the N-terminal regulatory domain of NDR kinase were used to identify and map a specific interaction between Mob1 and this kinase. The chemical shift changes indicate that the main interaction occurs on the acidic and conserved surface of Mob1. This surface was previously hypothesized to be the interaction surface according to the X-ray structure and was identified as functionally important in yeast. Our data suggest that the NDR kinase is a functional Dbf2 homologue in animal cells and contributes to the understanding of the molecular function of Mob1 proteins. NMR solution structure of Mob1, a mitotic exit network protein and its interaction with an NDR kinase peptide.,Ponchon L, Dumas C, Kajava AV, Fesquet D, Padilla A J Mol Biol. 2004 Mar 12;337(1):167-82. PMID:15001360[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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