5le0: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 5le0 is ~~ON HOLD until Paper~~ Publication

==MICAL1 Cterminal domain==

== Structural highlights ==

<table><tr><td colspan='2'>[[5le0]] is a 1 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=5LE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LE0 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]] 3.3Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=5le0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5le0 OCA], [https://pdbe.org/5le0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5le0 RCSB], [https://www.ebi.ac.uk/pdbsum/5le0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5le0 ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/MICA1_HUMAN MICA1_HUMAN] Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin. Acts by modifying actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization (Probable). Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. Also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L; acts by antagonizing STK38 and STK38L activation by MST1/STK4.<ref>PMID:18305261</ref> <ref>PMID:21864500</ref>

== Publication Abstract from PubMed ==

Cytokinetic abscission, the terminal step of cell division, crucially depends on the local constriction of ESCRT-III helices after cytoskeleton disassembly. While the microtubules of the intercellular bridge are cut by the ESCRT-associated enzyme Spastin, the mechanism that clears F-actin at the abscission site is unknown. Here we show that oxidation-mediated depolymerization of actin by the redox enzyme MICAL1 is key for ESCRT-III recruitment and successful abscission. MICAL1 is recruited to the abscission site by the Rab35 GTPase through a direct interaction with a flat three-helix domain found in MICAL1 C terminus. Mechanistically, in vitro assays on single actin filaments demonstrate that MICAL1 is activated by Rab35. Moreover, in our experimental conditions, MICAL1 does not act as a severing enzyme, as initially thought, but instead induces F-actin depolymerization from both ends. Our work reveals an unexpected role for oxidoreduction in triggering local actin depolymerization to control a fundamental step of cell division.

~~Authors~~:

Oxidation of F-actin controls the terminal steps of cytokinesis.,Fremont S, Hammich H, Bai J, Wioland H, Klinkert K, Rocancourt M, Kikuti C, Stroebel D, Romet-Lemonne G, Pylypenko O, Houdusse A, Echard A Nat Commun. 2017 Feb 23;8:14528. doi: 10.1038/ncomms14528. PMID:28230050<ref>PMID:28230050</ref>

~~Description~~:

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

[[Category: ~~Unreleased~~ Structures]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Hammich H]]

[[Category: Houdusse A]]

[[Category: Pylypenko O]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5le0 is ON HOLD  until Paper Publication
+==MICAL1 Cterminal domain==
+<StructureSection load='5le0' size='340' side='right'caption='[[5le0]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5le0]] is a 1 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=5LE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LE0 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]] 3.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=5le0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5le0 OCA], [https://pdbe.org/5le0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5le0 RCSB], [https://www.ebi.ac.uk/pdbsum/5le0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5le0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MICA1_HUMAN MICA1_HUMAN] Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin. Acts by modifying actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization (Probable). Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. Also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L; acts by antagonizing STK38 and STK38L activation by MST1/STK4.<ref>PMID:18305261</ref> <ref>PMID:21864500</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Cytokinetic abscission, the terminal step of cell division, crucially depends on the local constriction of ESCRT-III helices after cytoskeleton disassembly. While the microtubules of the intercellular bridge are cut by the ESCRT-associated enzyme Spastin, the mechanism that clears F-actin at the abscission site is unknown. Here we show that oxidation-mediated depolymerization of actin by the redox enzyme MICAL1 is key for ESCRT-III recruitment and successful abscission. MICAL1 is recruited to the abscission site by the Rab35 GTPase through a direct interaction with a flat three-helix domain found in MICAL1 C terminus. Mechanistically, in vitro assays on single actin filaments demonstrate that MICAL1 is activated by Rab35. Moreover, in our experimental conditions, MICAL1 does not act as a severing enzyme, as initially thought, but instead induces F-actin depolymerization from both ends. Our work reveals an unexpected role for oxidoreduction in triggering local actin depolymerization to control a fundamental step of cell division.
-Authors:
+Oxidation of F-actin controls the terminal steps of cytokinesis.,Fremont S, Hammich H, Bai J, Wioland H, Klinkert K, Rocancourt M, Kikuti C, Stroebel D, Romet-Lemonne G, Pylypenko O, Houdusse A, Echard A Nat Commun. 2017 Feb 23;8:14528. doi: 10.1038/ncomms14528. PMID:28230050<ref>PMID:28230050</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5le0" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Hammich H]]
+[[Category: Houdusse A]]
+[[Category: Pylypenko O]]