4d0a
From Proteopedia
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| - | ''' | + | ==3D EM map of the sodium proton antiporter MjNhaP1 from Methanocaldococcus jannaschii== |
| + | <StructureSection load='4d0a' size='340' side='right' caption='[[4d0a]], [[Resolution|resolution]] 6.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4d0a]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D0A FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d0a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d0a RCSB], [http://www.ebi.ac.uk/pdbsum/4d0a PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sodium/proton antiporters are essential for sodium and pH homeostasis and play a major role in human health and disease. We determined the structures of the archaeal sodium/proton antiporter MjNhaP1 in two complementary states. The inward-open state was obtained by x-ray crystallography in the presence of sodium at pH8, where the transporter is highly active. The outward-open state was obtained by electron crystallography without sodium at pH4, where MjNhaP1 is inactive. Comparison of both structures reveals a 7{degree sign} tilt of the 6 helix bundle. 22Na+ uptake measurements indicate non-cooperative transport with an activity maximum at pH7.5. We conclude that binding of a Na+ ion from the outside induces helix movements that close the extracellular cavity, open the cytoplasmic funnel, and result in a ~5 A vertical relocation of the ion binding site to release the substrate ion into the cytoplasm. | ||
| - | + | Structure and transport mechanism of the sodium/protonantiporter MjNhaP1.,Paulino C, Wohlert D, Kapotova E, Yildiz O, Kuhlbrandt W Elife. 2014 Nov 26;3. doi: 10.7554/eLife.03583. PMID:25426803<ref>PMID:25426803</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Kuhlbrandt, W]] | ||
| + | [[Category: Paulino, C]] | ||
| + | [[Category: Woehlert, D]] | ||
| + | [[Category: Yildiz, O]] | ||
| + | [[Category: Antiporter]] | ||
| + | [[Category: Cpa]] | ||
| + | [[Category: Exchanger]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Transport protein]] | ||
| + | [[Category: Transporter]] | ||
Revision as of 16:03, 10 December 2014
3D EM map of the sodium proton antiporter MjNhaP1 from Methanocaldococcus jannaschii
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