4d0a: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==3D EM map of the sodium proton antiporter MjNhaP1 from Methanocaldococcus jannaschii==

== 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>

== 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.

~~The entry 4d0a is ON HOLD~~

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>

~~Authors~~: Paulino, C., Woehlert, D., Yildiz, O~~., Kuhlbrandt, W.~~

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

</div>

~~Description~~: ~~3D EM map of the sodium proton antiporter MjNhaP1 from Methanocaldococcus jannaschii~~

== 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]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==3D EM map of the sodium proton antiporter MjNhaP1 from Methanocaldococcus jannaschii==
+<StructureSection load='4d0a' size='340' side='right' caption='[[4d0a]], [[Resolution|resolution]] 6.00&Aring;' 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.
-The entry 4d0a is ON HOLD
+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>
-Authors: Paulino, C., Woehlert, D., Yildiz, O., Kuhlbrandt, W.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: 3D EM map of the sodium proton antiporter MjNhaP1 from Methanocaldococcus jannaschii
+== 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]]