6mn6: Difference between revisions
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==Crystal structure of the cytosolic domain of human CNNM3== | |||
<StructureSection load='6mn6' size='340' side='right'caption='[[6mn6]], [[Resolution|resolution]] 3.36Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6mn6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MN6 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]] 3.36Å</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=6mn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mn6 OCA], [https://pdbe.org/6mn6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mn6 RCSB], [https://www.ebi.ac.uk/pdbsum/6mn6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mn6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6mn6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen YS]] | |||
[[Category: Gehring K]] | |||
[[Category: Yang M]] | |||
Latest revision as of 06:34, 11 October 2023
Crystal structure of the cytosolic domain of human CNNM3
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