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==Crystal Structure of ApcT Transporter Bound to 7F11 Monoclonal Fab Fragment==
==Crystal Structure of ApcT Transporter Bound to 7F11 Monoclonal Fab Fragment==
<StructureSection load='3gi9' size='340' side='right' caption='[[3gi9]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
<StructureSection load='3gi9' size='340' side='right' caption='[[3gi9]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3gi9]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GI9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GI9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3gi9]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GI9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GI9 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gi8|3gi8]], [[3gia|3gia]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gi8|3gi8]], [[3gia|3gia]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MJ0609 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MJ0609 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067])</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=3gi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gi9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gi9 RCSB], [http://www.ebi.ac.uk/pdbsum/3gi9 PDBsum]</span></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=3gi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gi9 OCA], [http://pdbe.org/3gi9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gi9 RCSB], [http://www.ebi.ac.uk/pdbsum/3gi9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gi9 ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3gi9 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3gi9" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Monoclonal Antibody|Monoclonal Antibody]]
*[[3D structures of monoclonal antibody|3D structures of monoclonal antibody]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Methanocaldococcus jannaschii]]
[[Category: Atcc 43067]]
[[Category: Mus musculus]]
[[Category: Lk3 transgenic mice]]
[[Category: Goehring, A S]]
[[Category: Goehring, A S]]
[[Category: Gouaux, E]]
[[Category: Gouaux, E]]

Revision as of 18:49, 11 August 2016

Crystal Structure of ApcT Transporter Bound to 7F11 Monoclonal Fab FragmentCrystal Structure of ApcT Transporter Bound to 7F11 Monoclonal Fab Fragment

Structural highlights

3gi9 is a 3 chain structure with sequence from Atcc 43067 and Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:MJ0609 (ATCC 43067)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Amino acid, polyamine, and organocation (APC) transporters are secondary transporters that play essential roles in nutrient uptake, neurotransmitter recycling, ionic homeostasis, and regulation of cell volume. Here, we present the crystal structure of apo-ApcT, a proton-coupled broad-specificity amino acid transporter, at 2.35 A resolution. The structure contains 12 transmembrane helices, with the first 10 consisting of an inverted structural repeat of 5 transmembrane helices like LeuT. The ApcT structure reveals an inward-facing, apo state and an amine moiety of Lys158 located in a position equivalent to the Na2 ion of LeuT. We propose that Lys158 is central to proton-coupled transport and that the amine group serves the same functional role as the Na2 ion in LeuT, thus demonstrating common principles among proton- and sodium-coupled transporters.

Structure and Mechanism of a Na+ Independent Amino Acid Transporter.,Shaffer PL, Goehring A, Shankaranarayanan A, Gouaux E Science. 2009 Jul 22. PMID:19608859[1]

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

See Also

References

  1. Shaffer PL, Goehring A, Shankaranarayanan A, Gouaux E. Structure and Mechanism of a Na+ Independent Amino Acid Transporter. Science. 2009 Jul 22. PMID:19608859

3gi9, resolution 2.48Å

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