6r2q

Structure of the Mtr complex

spinqualitylabelsall models 6r2q, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.697Å Ligands: CA, HEC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed A growing number of bacteria are recognized to conduct electrons across their cell envelope, and yet molecular details of the mechanisms supporting this process remain unknown. Here, we report the atomic structure of an outer membrane spanning protein complex, MtrAB, that is representative of a protein family known to transport electrons between the interior and exterior environments of phylogenetically and metabolically diverse microorganisms. The structure is revealed as a naturally insulated biomolecular wire possessing a 10-heme cytochrome, MtrA, insulated from the membrane lipidic environment by embedding within a 26 strand beta-barrel formed by MtrB. MtrAB forms an intimate connection with an extracellular 10-heme cytochrome, MtrC, which presents its hemes across a large surface area for electrical contact with extracellular redox partners, including transition metals and electrodes. The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire.,Edwards MJ, White GF, Butt JN, Richardson DJ, Clarke TA Cell. 2020 Apr 8. pii: S0092-8674(20)30325-1. doi: 10.1016/j.cell.2020.03.032. PMID:32289252 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cystathionine β-synthase 3D structures

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