3chg

<StructureSection load='3chg' size='340' side='right' caption='[[3chg]], [[Resolution|resolution]] 2.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[3chg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CHG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CHG FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=313:(DIMETHYL-LAMBDA~4~-SULFANYL)ACETIC+ACID'>313</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2b4l|2b4l]], [[2b4m|2b4m]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">opuAC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</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=3chg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3chg OCA], [http://pdbe.org/3chg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3chg RCSB], [http://www.ebi.ac.uk/pdbsum/3chg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3chg ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/OPUAC_BACSU OPUAC_BACSU]] Involved in a multicomponent binding-protein-dependent transport system for glycine betaine.<ref>PMID:7622480</ref> <ref>PMID:8752321</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/3chg_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

In the soil bacterium Bacillus subtilis, five transport systems work in concert to mediate the import of various compatible solutes that counteract the deleterious effects of increases in the osmolarity of the environment. Among these five systems, the ABC transporter OpuA, which catalyzes the import of glycine betaine and proline betaine, has been studied in detail in the past. Here, we demonstrate that OpuA is capable of importing the sulfobetaine dimethylsulfonioacetate (DMSA). Since OpuA is a classic ABC importer that relies on a substrate-binding protein priming the transporter with specificity and selectivity, we analyzed the OpuA-binding protein OpuAC by structural and mutational means with respect to DMSA binding. The determined crystal structure of OpuAC in complex with DMSA at a 2.8-A resolution and a detailed mutational analysis of these residues revealed a hierarchy within the amino acids participating in substrate binding. This finding is different from those for other binding proteins that recognize compatible solutes. Furthermore, important principles that enable OpuAC to specifically bind various compatible solutes were uncovered.

 

<div class="pdbe-citations 3chg" style="background-color:#fffaf0;"></div>

[[Category: Bacillus globigii migula 1900]]

[[Category: Bremer, E]]

[[Category: Hoing, M]]

[[Category: Jebbar, M]]

[[Category: Lecher, J]]

[[Category: Schmitt, L]]

[[Category: Smits, S H.J]]

[[Category: Transport protein]]