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10.1038/s41467-021-24282-7 http://scihub22266oqcxt.onion/10.1038/s41467-021-24282-7 34188059!8242095!34188059     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=34188059&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2021 ; 12 (1): 4028 Nephropedia Template TP {{tp|p=34188059|t=2021. Crystal structure of an archaeal CorB magnesium transporter |pdf=|usr=}}{{34188059}} gab.com Text Crystal structure of an archaeal CorB magnesium transporter JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=34188059 #FOAvip CNNM/CorB proteins are a broadly conserved family of integral membrane proteins with close to 90,000 protein sequences known. They are associated with Mg(2+) transport but it is not known if they mediate transport themselves or regulate other transporters. Here, we determine the crystal structure of an archaeal CorB protein in two conformations (apo and Mg(2+)-ATP bound). The transmembrane DUF21 domain exists in an inward-facing conformation with a Mg(2+) ion coordinated by a conserved pi-helix. In the absence of Mg(2+)-ATP, the CBS-pair domain adopts an elongated dimeric configuration with previously unobserved domain-domain contacts. Hydrogen-deuterium exchange mass spectrometry, analytical ultracentrifugation, and molecular dynamics experiments support a role of the structural rearrangements in mediating Mg(2+)-ATP sensing. Lastly, we use an in vitro, liposome-based assay to demonstrate direct Mg(2+) transport by CorB proteins. These structural and functional insights provide a framework for understanding function of CNNMs in Mg(2+) transport and associated diseases. Twit Text FOAVip Crystal structure of an archaeal CorB magnesium transporter ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=34188059 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34188059 #FOAvip English Wikipedia <ref>{{Cite pmid|34188059}}</ref> Crystal structure of an archaeal CorB magnesium transporter #MMPMID34188059 Chen YS; Kozlov G; Moeller BE; Rohaim A; Fakih R; Roux B; Burke JE; Gehring K Nat Commun 2021[Jun]; 12 (1): 4028 PMID34188059show ga CNNM/CorB proteins are a broadly conserved family of integral membrane proteins with close to 90,000 protein sequences known. They are associated with Mg(2+) transport but it is not known if they mediate transport themselves or regulate other transporters. Here, we determine the crystal structure of an archaeal CorB protein in two conformations (apo and Mg(2+)-ATP bound). The transmembrane DUF21 domain exists in an inward-facing conformation with a Mg(2+) ion coordinated by a conserved pi-helix. In the absence of Mg(2+)-ATP, the CBS-pair domain adopts an elongated dimeric configuration with previously unobserved domain-domain contacts. Hydrogen-deuterium exchange mass spectrometry, analytical ultracentrifugation, and molecular dynamics experiments support a role of the structural rearrangements in mediating Mg(2+)-ATP sensing. Lastly, we use an in vitro, liposome-based assay to demonstrate direct Mg(2+) transport by CorB proteins. These structural and functional insights provide a framework for understanding function of CNNMs in Mg(2+) transport and associated diseases. |Amino Acid Sequence[MESH] |Cation Transport Proteins/genetics/*metabolism[MESH] |Crystallography, X-Ray[MESH] |Deuterium Exchange Measurement[MESH] |Hydrogenophilaceae/*metabolism[MESH] |Magnesium/*metabolism[MESH] |Methanomicrobiaceae/*metabolism[MESH] |Molecular Dynamics Simulation[MESH] |Protein Conformation[MESH]Crystal structure of an archaeal CorB magnesium transporter (epmc).pdf DeepDyve Pubget Overpricing