6cse: Difference between revisions

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-'''Unreleased structure'''
-The entry 6cse is ON HOLD  until Paper Publication
+==Crystal structure of sodium/alanine symporter AgcS with L-alanine bound==
+<StructureSection load='6cse' size='340' side='right' caption='[[6cse]], [[Resolution|resolution]] 3.24&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6cse]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Metmp Metmp] 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=6CSE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CSE FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">agcS, MMP1511 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=267377 METMP])</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=6cse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cse OCA], [http://pdbe.org/6cse PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cse RCSB], [http://www.ebi.ac.uk/pdbsum/6cse PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cse ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/AGCS_METMP AGCS_METMP]] Probably functions as a sodium/L- and D-alanine symporter for alanine uptake.<ref>PMID:15659675</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The amino acid, polyamine, and organocation (APC) superfamily is the second largest superfamily of membrane proteins forming secondary transporters that move a range of organic molecules across the cell membrane. Each transporter in the APC superfamily is specific for a unique subset of substrates, even if they possess a similar structural fold. The mechanism of substrate selectivity remains, by and large, elusive. Here, we report two crystal structures of an APC member from Methanococcus maripaludis, the alanine or glycine:cation symporter (AgcS), with l- or d-alanine bound. Structural analysis combined with site-directed mutagenesis and functional studies inform on substrate binding, specificity, and modulation of the AgcS family and reveal key structural features that allow this transporter to accommodate glycine and alanine while excluding all other amino acids. Mutation of key residues in the substrate binding site expand the selectivity to include valine and leucine. These studies provide initial insights into substrate selectivity in AgcS symporters.
-Authors:
+Structural basis for substrate binding and specificity of a sodium-alanine symporter AgcS.,Ma J, Lei HT, Reyes FE, Sanchez-Martinez S, Sarhan MF, Hattne J, Gonen T Proc Natl Acad Sci U S A. 2019 Jan 18. pii: 1806206116. doi:, 10.1073/pnas.1806206116. PMID:30659158<ref>PMID:30659158</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6cse" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Metmp]]
+[[Category: Mus musculus]]
+[[Category: Gonen, T]]
+[[Category: Ma, J]]
+[[Category: Reyes, F E]]
+[[Category: Membrane protein]]