6csf: Difference between revisions
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==Crystal structure of sodium/alanine symporter AgcS with D-alanine bound== | |||
<StructureSection load='6csf' size='340' side='right' caption='[[6csf]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6csf]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] 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=6CSF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CSF FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=6csf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6csf OCA], [http://pdbe.org/6csf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6csf RCSB], [http://www.ebi.ac.uk/pdbsum/6csf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6csf 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6csf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Mus musculus]] | |||
[[Category: Gonen, T]] | |||
[[Category: Ma, J]] | |||
[[Category: Reyes, F E]] | |||
[[Category: Membrane protein]] | |||
Revision as of 11:15, 30 January 2019
Crystal structure of sodium/alanine symporter AgcS with D-alanine boundCrystal structure of sodium/alanine symporter AgcS with D-alanine bound
Structural highlights
Function[AGCS_METMP] Probably functions as a sodium/L- and D-alanine symporter for alanine uptake.[1] Publication Abstract from PubMedThe 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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