3chg: Difference between revisions

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==The compatible solute-binding protein OpuAC from Bacillus subtilis in complex with DMSA==
==The compatible solute-binding protein OpuAC from Bacillus subtilis in complex with DMSA==
<StructureSection load='3chg' size='340' side='right' caption='[[3chg]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='3chg' size='340' side='right'caption='[[3chg]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3chg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. 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>
<table><tr><td colspan='2'>[[3chg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3CHG FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=313:(DIMETHYL-LAMBDA~4~-SULFANYL)ACETIC+ACID'>313</scene><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]] 2.8&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2b4l|2b4l]], [[2b4m|2b4m]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=313:(DIMETHYL-LAMBDA~4~-SULFANYL)ACETIC+ACID'>313</scene></td></tr>
<tr><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 subtilis])</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=3chg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3chg OCA], [https://pdbe.org/3chg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3chg RCSB], [https://www.ebi.ac.uk/pdbsum/3chg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3chg ProSAT]</span></td></tr>
<tr><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://www.rcsb.org/pdb/explore.do?structureId=3chg RCSB], [http://www.ebi.ac.uk/pdbsum/3chg PDBsum]</span></td></tr>
</table>
<table>
== Function ==
[https://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>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/3chg_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/3chg_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3chg ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.
The compatible-solute-binding protein OpuAC from Bacillus subtilis: ligand binding, site-directed mutagenesis, and crystallographic studies.,Smits SH, Hoing M, Lecher J, Jebbar M, Schmitt L, Bremer E J Bacteriol. 2008 Aug;190(16):5663-71. Epub 2008 Jun 20. PMID:18567662<ref>PMID:18567662</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==See Also==
</div>
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Bremer, E.]]
[[Category: Large Structures]]
[[Category: Hoing, M.]]
[[Category: Bremer E]]
[[Category: Jebbar, M.]]
[[Category: Hoing M]]
[[Category: Lecher, J.]]
[[Category: Jebbar M]]
[[Category: Schmitt, L.]]
[[Category: Lecher J]]
[[Category: Smits, S H.J.]]
[[Category: Schmitt L]]
[[Category: Ligand binding protein]]
[[Category: Smits SHJ]]
[[Category: Substrate binding protein]]
[[Category: Transport protein]]

Latest revision as of 12:35, 21 February 2024

The compatible solute-binding protein OpuAC from Bacillus subtilis in complex with DMSAThe compatible solute-binding protein OpuAC from Bacillus subtilis in complex with DMSA

Structural highlights

3chg is a 4 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OPUAC_BACSU Involved in a multicomponent binding-protein-dependent transport system for glycine betaine.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Kempf B, Bremer E. OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis. J Biol Chem. 1995 Jul 14;270(28):16701-13. PMID:7622480
  2. Kappes RM, Kempf B, Bremer E. Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: characterization of OpuD. J Bacteriol. 1996 Sep;178(17):5071-9. PMID:8752321

3chg, resolution 2.80Å

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