6mn6: Difference between revisions

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== Function ==

[[http://www.uniprot.org/uniprot/CNNM3_HUMAN CNNM3_HUMAN]] Probable metal transporter.

== Publication Abstract from PubMed ==

The family of cystathionine-beta-synthase (CBS)-pair domain divalent metal cation transport mediators (CNNMs) is composed of four integral membrane proteins associated with Mg(2+) transport. Structurally, CNNMs contain large cytosolic regions composed of a CBS-pair and a cyclic nucleotide-binding homology (CNBH) domain. How these regulate Mg(2+) transport activity is unknown. Here, we determined the crystal structures of cytosolic fragments in two conformations: Mg(2+)-ATP-analog bound and ligand free. The structures reveal open and closed conformations with functionally important contacts not observed in structures of the individual domains. We also identified a second Mg(2+)-binding region in the CBS-pair domain and a different dimerization interface for the CNBH domain. Analytical ultracentrifugation and isothermal titration calorimetry experiments revealed a tight correlation between Mg(2+)-ATP binding and protein dimerization. Mutations that blocked either function prevented cellular Mg(2+) efflux activity. The results suggest Mg(2+) efflux is regulated by conformational changes associated with Mg(2+)-ATP binding to CNNM CBS-pair domains.

Mg(2+)-ATP Sensing in CNNM, a Putative Magnesium Transporter.,Chen YS, Kozlov G, Fakih R, Yang M, Zhang Z, Kovrigin EL, Gehring K Structure. 2019 Dec 10. pii: S0969-2126(19)30434-4. doi:, 10.1016/j.str.2019.11.016. PMID:31864811<ref>PMID:31864811</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

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 == Function ==
 [[http://www.uniprot.org/uniprot/CNNM3_HUMAN CNNM3_HUMAN]] Probable metal transporter.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The family of cystathionine-beta-synthase (CBS)-pair domain divalent metal cation transport mediators (CNNMs) is composed of four integral membrane proteins associated with Mg(2+) transport. Structurally, CNNMs contain large cytosolic regions composed of a CBS-pair and a cyclic nucleotide-binding homology (CNBH) domain. How these regulate Mg(2+) transport activity is unknown. Here, we determined the crystal structures of cytosolic fragments in two conformations: Mg(2+)-ATP-analog bound and ligand free. The structures reveal open and closed conformations with functionally important contacts not observed in structures of the individual domains. We also identified a second Mg(2+)-binding region in the CBS-pair domain and a different dimerization interface for the CNBH domain. Analytical ultracentrifugation and isothermal titration calorimetry experiments revealed a tight correlation between Mg(2+)-ATP binding and protein dimerization. Mutations that blocked either function prevented cellular Mg(2+) efflux activity. The results suggest Mg(2+) efflux is regulated by conformational changes associated with Mg(2+)-ATP binding to CNNM CBS-pair domains.
+Mg(2+)-ATP Sensing in CNNM, a Putative Magnesium Transporter.,Chen YS, Kozlov G, Fakih R, Yang M, Zhang Z, Kovrigin EL, Gehring K Structure. 2019 Dec 10. pii: S0969-2126(19)30434-4. doi:, 10.1016/j.str.2019.11.016. PMID:31864811<ref>PMID:31864811</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6mn6" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>