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2hjn

From Proteopedia

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Structural and functional analysis of Saccharomyces cerevisiae Mob1

Structural highlights

2hjn is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MOB1_YEAST] Functions as an activator subunit for the DBF2 protein kinase. Binds to DBF2, which is required for the phosphorylation and activation of DBF2 by the upstream kinase CDC15 in late anaphase. DBF2-MOB1 is part of the mitotic exit network (MEN) signaling cascade, which regulates release from the nucleus and activity of phosphatase CDC14. Required for inactivation of mitotic cyclin-dependent kinase for exit from mitosis, cytokinesis and G1 gene transcription.^[1] ^[2] ^[3]

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

The Mob proteins function as activator subunits for the Dbf2/Dbf20 family of protein kinases. Human and Xenopus Mob1 protein structures corresponding to the most conserved C-terminal core, but lacking the variable N-terminal region, have been reported and provide a framework for understanding the mechanism of Dbf2/Dbf20 regulation. Here, we report the 2.0 A X-ray crystal structure of Saccharomyces cerevisiae Mob1 containing both the conserved C-terminal core and the variable N-terminal region. Within the N-terminal region, three novel structural elements are observed; namely, an alpha-helix denoted H0, a strand-like element denoted S0 and a short beta strand denoted S-1. Helix H0 associates in an intermolecular manner with a second Mob1 molecule to form a Mob1 homodimer. Strand S0 binds to the core domain in an intramolecular manner across a putative Dbf2 binding site mapped by Mob1 temperature-sensitive alleles and NMR binding experiments. In vivo functional analysis demonstrates that Mob1 mutants that target helix H0 or its reciprocal binding site are biologically compromised. The N-terminal region of Mob1 thus contains structural elements that are functionally important.

Structural and functional analysis of Saccharomyces cerevisiae Mob1.,Mrkobrada S, Boucher L, Ceccarelli DF, Tyers M, Sicheri F J Mol Biol. 2006 Sep 22;362(3):430-40. Epub 2006 Aug 24. PMID:16934835^[4]

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

References

↑ Luca FC, Mody M, Kurischko C, Roof DM, Giddings TH, Winey M. Saccharomyces cerevisiae Mob1p is required for cytokinesis and mitotic exit. Mol Cell Biol. 2001 Oct;21(20):6972-83. PMID:11564880 doi:http://dx.doi.org/10.1128/MCB.21.20.6972-6983.2001
↑ Mah AS, Jang J, Deshaies RJ. Protein kinase Cdc15 activates the Dbf2-Mob1 kinase complex. Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7325-30. Epub 2001 Jun 12. PMID:11404483 doi:http://dx.doi.org/10.1073/pnas.141098998
↑ Stoepel J, Ottey MA, Kurischko C, Hieter P, Luca FC. The mitotic exit network Mob1p-Dbf2p kinase complex localizes to the nucleus and regulates passenger protein localization. Mol Biol Cell. 2005 Dec;16(12):5465-79. Epub 2005 Sep 21. PMID:16176976 doi:http://dx.doi.org/E05-04-0337
↑ Mrkobrada S, Boucher L, Ceccarelli DF, Tyers M, Sicheri F. Structural and functional analysis of Saccharomyces cerevisiae Mob1. J Mol Biol. 2006 Sep 22;362(3):430-40. Epub 2006 Aug 24. PMID:16934835 doi:10.1016/j.jmb.2006.07.007

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Structural and functional analysis of Saccharomyces cerevisiae Mob1==
-<StructureSection load='2hjn' size='340' side='right' caption='[[2hjn]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='2hjn' size='340' side='right'caption='[[2hjn]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2hjn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HJN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HJN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2hjn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HJN FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2hjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hjn OCA], [http://pdbe.org/2hjn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hjn RCSB], [http://www.ebi.ac.uk/pdbsum/2hjn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hjn ProSAT]</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=2hjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hjn OCA], [https://pdbe.org/2hjn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hjn RCSB], [https://www.ebi.ac.uk/pdbsum/2hjn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hjn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MOB1_YEAST MOB1_YEAST]] Functions as an activator subunit for the DBF2 protein kinase. Binds to DBF2, which is required for the phosphorylation and activation of DBF2 by the upstream kinase CDC15 in late anaphase. DBF2-MOB1 is part of the mitotic exit network (MEN) signaling cascade, which regulates release from the nucleus and activity of phosphatase CDC14. Required for inactivation of mitotic cyclin-dependent kinase for exit from mitosis, cytokinesis and G1 gene transcription.<ref>PMID:11564880</ref> <ref>PMID:11404483</ref> <ref>PMID:16176976</ref>
+[[https://www.uniprot.org/uniprot/MOB1_YEAST MOB1_YEAST]] Functions as an activator subunit for the DBF2 protein kinase. Binds to DBF2, which is required for the phosphorylation and activation of DBF2 by the upstream kinase CDC15 in late anaphase. DBF2-MOB1 is part of the mitotic exit network (MEN) signaling cascade, which regulates release from the nucleus and activity of phosphatase CDC14. Required for inactivation of mitotic cyclin-dependent kinase for exit from mitosis, cytokinesis and G1 gene transcription.<ref>PMID:11564880</ref> <ref>PMID:11404483</ref> <ref>PMID:16176976</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Ceccarelli, D F]]

2hjn

From Proteopedia

Current revision

Structural and functional analysis of Saccharomyces cerevisiae Mob1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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