View source for 3gi9


==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=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3gi9]] is a 3 chain structure. 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>
<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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gi/3gi9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=3gi9 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:19608859</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3gi9" style="background-color:#fffaf0;"></div>

==See Also==
*[[3D structures of monoclonal antibody|3D structures of monoclonal antibody]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Goehring, A S]]
[[Category: Gouaux, E]]
[[Category: NYCOMPS, New York Consortium on Membrane Protein Structure]]
[[Category: Shaffer, P L]]
[[Category: Shankaranarayanan, A]]
[[Category: Antibody]]
[[Category: Cell membrane]]
[[Category: Membrane]]
[[Category: Membrane protein]]
[[Category: New york consortium on membrane protein structure]]
[[Category: Nycomp]]
[[Category: PSI, Protein structure initiative]]
[[Category: Structural genomic]]
[[Category: Transmembrane]]
[[Category: Transport protein]]
[[Category: Transporter]]