5ho5: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==MamB== | ==MamB== | ||
<StructureSection load='5ho5' size='340' side='right' caption='[[5ho5]], [[Resolution|resolution]] 1.99Å' scene=''> | <StructureSection load='5ho5' size='340' side='right'caption='[[5ho5]], [[Resolution|resolution]] 1.99Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ho5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[5ho5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Magsq Magsq]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HO5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HO5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mamB, MGMAQ_1061 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1288970 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mamB, MGMAQ_1061 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1288970 MAGSQ])</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=5ho5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ho5 OCA], [http://pdbe.org/5ho5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ho5 RCSB], [http://www.ebi.ac.uk/pdbsum/5ho5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ho5 ProSAT]</span></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=5ho5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ho5 OCA], [http://pdbe.org/5ho5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ho5 RCSB], [http://www.ebi.ac.uk/pdbsum/5ho5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ho5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| Line 21: | Line 21: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Magsq]] | |||
[[Category: Davidov, G]] | [[Category: Davidov, G]] | ||
[[Category: Keren, N]] | [[Category: Keren, N]] | ||
Revision as of 09:20, 16 October 2019
MamBMamB
Structural highlights
Publication Abstract from PubMedMagnetospirillum gryphiswaldense MSR-1 synthesizes membrane-enclosed magnetite (Fe3 O4 ) nanoparticles, magnetosomes, for magnetotaxis. Formation of these organelles involves a complex process comprising key steps which are governed by specific magnetosome-associated proteins. MamB, a cation diffusion facilitator (CDF) family member has been implicated in magnetosome-directed iron transport. However, deletion mutagenesis studies revealed that MamB is essential for the formation of magnetosome membrane vesicles, but its precise role remains elusive. In this study, we employed a multi-disciplinary approach to define the role of MamB during magnetosome formation. Using site-directed mutagenesis complemented by structural analyses, fluorescence microscopy and cryo-electron tomography, we show that MamB is most likely an active magnetosome-directed transporter serving two distinct, yet essential functions. First, MamB initiates magnetosome vesicle formation in a transport-independent process, probably by serving as a landmark protein. Second, MamB transport activity is required for magnetite nucleation. Furthermore, by determining the crystal structure of the MamB cytosolic C-terminal domain, we also provide mechanistic insight into transport regulation. Additionally, we present evidence that magnetosome vesicle growth and chain formation are independent of magnetite nucleation and magnetic interactions respectively. Together, our data provide novel insight into the role of the key bifunctional magnetosome protein MamB, and the early steps of magnetosome formation. The dual role of MamB in magnetosome membrane assembly and magnetite biomineralization.,Uebe R, Keren-Khadmy N, Zeytuni N, Katzmann E, Navon Y, Davidov G, Bitton R, Plitzko JM, Schuler D, Zarivach R Mol Microbiol. 2018 Feb;107(4):542-557. doi: 10.1111/mmi.13899. Epub 2018 Jan 9. PMID:29243866[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||