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==Structural characterization of a carbohydrate substrate binding protein from Streptococcus pneumoniae==
<StructureSection load='5mlt' size='340' side='right'caption='[[5mlt]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mlt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MLT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.61&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5mlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mlt OCA], [https://pdbe.org/5mlt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mlt RCSB], [https://www.ebi.ac.uk/pdbsum/5mlt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mlt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SBP92_STRPN SBP92_STRPN] Probably part of an ABC transporter complex involved in carbohydrate transport.<ref>PMID:28045395</ref> <ref>PMID:28994793</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Streptococcus pneumoniae is an opportunistic respiratory pathogen that remains a major cause of morbidity and mortality globally, with infants and the elderly at the highest risk. S. pneumoniae relies entirely on carbohydrates as a source of carbon and dedicates a third of all uptake systems to carbohydrate import. The structure of the carbohydrate-free substrate-binding protein SP0092 at 1.61 A resolution reveals it to belong to the newly proposed subclass G of substrate-binding proteins, with a ligand-binding pocket that is large enough to accommodate complex oligosaccharides. SP0092 is a dimer in solution and the crystal structure reveals a domain-swapped dimer with the monomer subunits in a closed conformation but in the absence of carbohydrate ligand. This closed conformation may be induced by dimer formation and could be used as a mechanism to regulate carbohydrate uptake.

Structural characterization of the Streptococcus pneumoniae carbohydrate substrate-binding protein SP0092.,Culurgioni S, Tang M, Walsh MA Acta Crystallogr F Struct Biol Commun. 2017 Jan 1;73(Pt 1):54-61. doi:, 10.1107/S2053230X16020252. Epub 2017 Jan 1. PMID:28045395<ref>PMID:28045395</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5mlt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae TIGR4]]
[[Category: Culurgioni S]]
[[Category: Tang M]]
[[Category: Walsh MA]]