4czb: Difference between revisions
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''' | ==Structure of the sodium proton antiporter MjNhaP1 from Methanocaldococcus jannaschii at pH 8.== | ||
<StructureSection load='4czb' size='340' side='right' caption='[[4czb]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4czb]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CZB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CZB FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cz8|4cz8]], [[4cz9|4cz9]], [[4cza|4cza]]</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=4czb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4czb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4czb RCSB], [http://www.ebi.ac.uk/pdbsum/4czb 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: Kapotova, E]] | |||
[[Category: Kuhlbrandt, W]] | |||
[[Category: Paulino, C]] | |||
[[Category: Woehlert, D]] | |||
[[Category: Yildiz, O]] | |||
[[Category: Antiporter]] | |||
[[Category: Cpa]] | |||
[[Category: Exchanger]] | |||
[[Category: Membrane protein]] | |||
[[Category: Transporter]] | |||
Revision as of 16:12, 10 December 2014
Structure of the sodium proton antiporter MjNhaP1 from Methanocaldococcus jannaschii at pH 8.
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