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5szg

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==Structure of the bMERB domain of Mical-3==
==Structure of the bMERB domain of Mical-3==
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<StructureSection load='5szg' size='340' side='right' caption='[[5szg]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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<StructureSection load='5szg' size='340' side='right'caption='[[5szg]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5szg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SZG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SZG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5szg]] 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=5SZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SZG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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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]] 2.7&#8491;</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<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=5szg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5szg OCA], [http://pdbe.org/5szg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5szg RCSB], [http://www.ebi.ac.uk/pdbsum/5szg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5szg ProSAT]</span></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=5szg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5szg OCA], [https://pdbe.org/5szg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5szg RCSB], [https://www.ebi.ac.uk/pdbsum/5szg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5szg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MICA3_HUMAN MICA3_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 (By similarity). Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process.<ref>PMID:21596566</ref>
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[https://www.uniprot.org/uniprot/MICA3_HUMAN MICA3_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 (By similarity). Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process.<ref>PMID:21596566</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In their active GTP-bound form, Rab proteins interact with proteins termed effector molecules. In this study we have thoroughly characterised a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. Within our study, we show that these effectors display a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and that some of the effector domains can bind two Rab proteins via separate binding sites. Structural analysis allowed us to explain the specificity towards Rab8 family members and the presence of two similar Rab binding sites that must have evolved via gene duplication. This study is the first to thoroughly characterise a Rab effector protein that contains two separate Rab binding sites within a single domain, allowing Micals and EHBPs to bind two Rabs simultaneously, thus suggesting previously unknown functions of these effector molecules in endosomal trafficking.
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bMERB domains are bivalent Rab8 family effectors evolved by gene duplication.,Rai A, Oprisko A, Campos J, Fu Y, Friese T, Itzen A, Goody RS, Gazdag EM, Muller MP Elife. 2016 Aug 23;5. pii: e18675. doi: 10.7554/eLife.18675. PMID:27552051<ref>PMID:27552051</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5szg" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Campos, J]]
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[[Category: Homo sapiens]]
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[[Category: Friese, T]]
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[[Category: Large Structures]]
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[[Category: Fu, Y]]
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[[Category: Campos J]]
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[[Category: Gazdag, E M]]
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[[Category: Friese T]]
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[[Category: Goody, R S]]
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[[Category: Fu Y]]
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[[Category: Itzen, A]]
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[[Category: Gazdag EM]]
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[[Category: Mueller, M P]]
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[[Category: Goody RS]]
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[[Category: Oprisko, A]]
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[[Category: Itzen A]]
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[[Category: Rai, A]]
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[[Category: Mueller MP]]
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[[Category: Duf3585]]
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[[Category: Oprisko A]]
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[[Category: Endocytosis]]
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[[Category: Rai A]]
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[[Category: Mical]]
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[[Category: Mical-3]]
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[[Category: Oxidoreductase]]
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[[Category: Rab effector]]
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Current revision

Structure of the bMERB domain of Mical-3

PDB ID 5szg

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