5mm3
From Proteopedia
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(New page: '''Unreleased structure''' The entry 5mm3 is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Unstructured MamC magnetite-binding protein located between two helices.== | |
| + | <StructureSection load='5mm3' size='340' side='right'caption='[[5mm3]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5mm3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Magnetospirillum_sp._XM-1 Magnetospirillum sp. XM-1] and [https://en.wikipedia.org/wiki/Methanosarcina_mazei Methanosarcina mazei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MM3 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]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</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=5mm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mm3 OCA], [https://pdbe.org/5mm3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mm3 RCSB], [https://www.ebi.ac.uk/pdbsum/5mm3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mm3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/MAMC_MAGSA MAMC_MAGSA] Probably involved in magnetite crystal growth (Probable). The lumenal domain may bind the magnetite crystals, affecting crystal size and shape (Probable).<ref>PMID:24961165</ref> <ref>PMID:26970040</ref> <ref>PMID:30405554</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Biomineralization is the process of mineral formation by organisms and involves the uptake of ions from the environment in order to produce minerals, with the process generally being mediated by proteins. Most proteins that are involved in mineral interactions are predicted to contain disordered regions containing large numbers of negatively charged amino acids. Magnetotactic bacteria, which are used as a model system for iron biomineralization, are Gram-negative bacteria that can navigate through geomagnetic fields using a specific organelle, the magnetosome. Each organelle comprises a membrane-enveloped magnetic nanoparticle, magnetite, the formation of which is controlled by a specific set of proteins. One of the most abundant of these proteins is MamC, a small magnetosome-associated integral membrane protein that contains two transmembrane alpha-helices connected by an approximately 21-amino-acid peptide. In vitro studies of this MamC peptide showed that it forms a helical structure that can interact with the magnetite surface and affect the size and shape of the growing crystal. Our results show that a disordered structure of the MamC magnetite-interacting component (MamC-MIC) abolishes its interaction with magnetite particles. Moreover, the size and shape of magnetite crystals grown in in vitro magnetite-precipitation experiments in the presence of this disordered peptide were different from the traits of crystals grown in the presence of other peptides or in the presence of the helical MIC. It is suggested that the helical structure of the MamC-MIC is important for its function during magnetite formation. | ||
| - | + | The importance of the helical structure of a MamC-derived magnetite-interacting peptide for its function in magnetite formation.,Nudelman H, Perez Gonzalez T, Kolushiva S, Widdrat M, Reichel V, Peigneux A, Davidov G, Bitton R, Faivre D, Jimenez-Lopez C, Zarivach R Acta Crystallogr D Struct Biol. 2018 Jan 1;74(Pt 1):10-20. doi:, 10.1107/S2059798317017491. Epub 2018 Jan 1. PMID:29372895<ref>PMID:29372895</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5mm3" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Magnetospirillum sp. XM-1]] | ||
| + | [[Category: Methanosarcina mazei]] | ||
| + | [[Category: Nudelman H]] | ||
| + | [[Category: Zarivach R]] | ||
Current revision
Unstructured MamC magnetite-binding protein located between two helices.
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