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5szh

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==Structure of human Rab1b in complex with the bMERB domain of Mical-cL==
==Structure of human Rab1b in complex with the bMERB domain of Mical-cL==
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<StructureSection load='5szh' size='340' side='right' caption='[[5szh]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='5szh' size='340' side='right'caption='[[5szh]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5szh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SZH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5szh]] 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=5SZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SZH 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=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.3&#8491;</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=5szh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5szh OCA], [http://pdbe.org/5szh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5szh RCSB], [http://www.ebi.ac.uk/pdbsum/5szh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5szh ProSAT]</span></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=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=5szh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5szh OCA], [https://pdbe.org/5szh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5szh RCSB], [https://www.ebi.ac.uk/pdbsum/5szh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5szh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MICLK_HUMAN MICLK_HUMAN]] May cooperate with MAPK1/ERK2 via an intracellular signal transduction pathway in the morphogenetic development of round spermatids to spermatozoa. [[http://www.uniprot.org/uniprot/RAB1B_HUMAN RAB1B_HUMAN]] Protein transport. Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments.<ref>PMID:9437002</ref>
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[https://www.uniprot.org/uniprot/MICA2_HUMAN MICA2_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).
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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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==See Also==
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*[[Ras-related protein Rab 3D structures|Ras-related protein Rab 3D structures]]
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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 5szh" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__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: Mueller, M P]]
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[[Category: Gazdag EM]]
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[[Category: Oprisko, A]]
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[[Category: Goody RS]]
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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-cl]]
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[[Category: Protein transport]]
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[[Category: Rab effector]]
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[[Category: Rab1b]]
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Current revision

Structure of human Rab1b in complex with the bMERB domain of Mical-cL

PDB ID 5szh

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