4m64: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4m64]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M64 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4m64]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M64 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4m64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m64 OCA], [https://pdbe.org/4m64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m64 RCSB], [https://www.ebi.ac.uk/pdbsum/4m64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m64 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4m64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m64 OCA], [https://pdbe.org/4m64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m64 RCSB], [https://www.ebi.ac.uk/pdbsum/4m64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m64 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/MELB_SALTY MELB_SALTY] Responsible for melibiose transport. It is capable of using hydrogen, sodium, and lithium cations as coupling cations for cotransport, depending on the particular sugar transported (symport system).
[https://www.uniprot.org/uniprot/MELB_SALTY MELB_SALTY] Responsible for melibiose transport. It is capable of using hydrogen, sodium, and lithium cations as coupling cations for cotransport, depending on the particular sugar transported (symport system).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The bacterial melibiose permease (MelB) belongs to the glycoside-pentoside-hexuronide:cation symporter family, a part of the major facilitator superfamily (MFS). Structural information regarding glycoside-pentoside-hexuronide:cation symporter family transporters and other Na(+)-coupled permeases within MFS has been lacking, although a wealth of biochemical and biophysical data are available. Here we present the three-dimensional crystal structures of Salmonella typhimurium MelBSt in two conformations, representing an outward partially occluded and an outward inactive state of MelBSt. MelB adopts a typical MFS fold and contains a previously unidentified cation-binding motif. Three conserved acidic residues form a pyramidal-shaped cation-binding site for Na(+), Li(+) or H(+), which is in close proximity to the sugar-binding site. Both cosubstrate-binding sites are mainly contributed by the residues from the amino-terminal domain. These two structures and the functional data presented here provide mechanistic insights into Na(+)/melibiose symport. We also postulate a structural foundation for the conformational cycling necessary for transport catalysed by MFS permeases in general.
Structure-based mechanism for Na(+)/melibiose symport by MelB.,Ethayathulla AS, Yousef MS, Amin A, Leblanc G, Kaback HR, Guan L Nat Commun. 2014 Jan 6;5:3009. doi: 10.1038/ncomms4009. PMID:24389923<ref>PMID:24389923</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4m64" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Symporter 3D structures|Symporter 3D structures]]
*[[Symporter 3D structures|Symporter 3D structures]]
== References ==
<references/>
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</StructureSection>
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