View source for 6h9m


==Coiled-coil domain-containing protein 90B residues 43-125 from Homo sapiens fused to a GCN4 adaptor==
<StructureSection load='6h9m' size='340' side='right'caption='[[6h9m]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6h9m]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H9M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H9M FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GCN4, AAS3, ARG9, YEL009C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6h9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h9m OCA], [http://pdbe.org/6h9m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h9m RCSB], [http://www.ebi.ac.uk/pdbsum/6h9m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h9m ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Membrane-bound coiled-coil proteins are important mediators of signaling, fusion, and scaffolding. Here, we delineate a heterogeneous group of trimeric membrane-anchored proteins in prokaryotes and eukaryotic organelles with a characteristic head-neck-stalk-anchor architecture, in which a membrane-anchored coiled-coil stalk projects an N-terminal head domain via a beta-layer neck. Based on sequence analysis, we identify different types of head domains and determine crystal structures of two representatives, the archaeal protein Kcr-0859 and the human CCDC90B, which possesses the most widespread head type. Using mitochondrial calcium uniporter regulator 1 (MCUR1), the functionally characterized paralog of CCDC90B, we study the role of individual domains, and find that the head interacts directly with the mitochondrial calcium uniporter (MCU) and is destabilized upon Ca(2+) binding. Our data provide structural details of a class of membrane-bound coiled-coil proteins and identify the conserved head domain of the most widespread type as a mediator of their function.

Characterization of MCU-Binding Proteins MCUR1 and CCDC90B - Representatives of a Protein Family Conserved in Prokaryotes and Eukaryotic Organelles.,Adlakha J, Karamichali I, Sangwallek J, Deiss S, Bar K, Coles M, Hartmann MD, Lupas AN, Hernandez Alvarez B Structure. 2018 Nov 23. pii: S0969-2126(18)30423-4. doi:, 10.1016/j.str.2018.11.004. PMID:30612859<ref>PMID:30612859</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6h9m" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Adlakha, J]]
[[Category: Albrecht, R]]
[[Category: Alvarez, B Hernandez]]
[[Category: Hartmann, M D]]
[[Category: Lupas, A N]]
[[Category: Beta-layer]]
[[Category: Coiled coil]]
[[Category: Membrane protein]]
[[Category: Mitochondrial membrane]]