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4czb

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'''Unreleased structure'''
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==Structure of the sodium proton antiporter MjNhaP1 from Methanocaldococcus jannaschii at pH 8.==
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<StructureSection load='4czb' size='340' side='right' caption='[[4czb]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cz8|4cz8]], [[4cz9|4cz9]], [[4cza|4cza]]</td></tr>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 4czb is ON HOLD until Paper Publication
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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>
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Authors: Woehlert, D., Paulino, C., Kapotova, E., Kuhlbrandt, W., Yildiz, O.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Structure of the sodium proton antiporter MjNhaP1 from Methanocaldococcus jannaschii at pH 8.
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Kapotova, E]]
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[[Category: Kuhlbrandt, W]]
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[[Category: Paulino, C]]
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[[Category: Woehlert, D]]
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[[Category: Yildiz, O]]
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[[Category: Antiporter]]
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[[Category: Cpa]]
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[[Category: Exchanger]]
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[[Category: Membrane protein]]
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[[Category: Transporter]]

Revision as of 16:12, 10 December 2014

Structure of the sodium proton antiporter MjNhaP1 from Methanocaldococcus jannaschii at pH 8.

4czb, resolution 3.50Å

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