3ppn: Difference between revisions

Latest revision as of 17:07, 1 November 2023

Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC

Structural highlights

3ppn is a 2 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 2.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OPUCC_BACSU Member of a high affinity multicomponent binding-protein-dependent transport system for glycine betaine, carnitine, and choline.^[1] ^[2]

Publication Abstract from PubMed

The compatible solute ATP-binding cassette (ABC) transporters are indispensable for acquiring a variety of compatible solutes under osmotic stress in Bacillus subtilis. The substrate-binding protein OpuCC of the ABC transporter OpuC can recognize a broad spectrum of compatible solutes, compared to its 70% sequence-identical paralog OpuBC that can solely bind choline. To explore the structural basis of this difference of substrate specificity, we determined crystal structures of OpuCC in the apo-form and in complex with carnitine, glycine betaine, choline and ectoine, respectively. OpuCC is composed of two alpha/beta/alpha globular sandwich domains linked by two hinge regions, with substrate-binding pocket located at the inter-domain cleft. Upon substrate-binding, the two domains shift towards each other to trap the substrate. Comparative structural analysis revealed a plastic pocket that fits various compatible solutes, which attributes the multiple-substrate binding property to OpuCC. This plasticity is a gain-of-function via a single-residue mutation of Thr94 in OpuCC versus Asp96 in OpuBC.

Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC.,Du Y, Shi WW, He YX, Yang YH, Zhou CZ, Chen Y Biochem J. 2011 Mar 3. PMID:21366542^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kappes RM, Kempf B, Kneip S, Boch J, Gade J, Meier-Wagner J, Bremer E. Two evolutionarily closely related ABC transporters mediate the uptake of choline for synthesis of the osmoprotectant glycine betaine in Bacillus subtilis. Mol Microbiol. 1999 Apr;32(1):203-16. PMID:10216873
↑ 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
↑ Du Y, Shi WW, He YX, Yang YH, Zhou CZ, Chen Y. Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC. Biochem J. 2011 Mar 3. PMID:21366542 doi:10.1042/BJ20102097

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Kappes RM, Kempf B, Kneip S, Boch J, Gade J, Meier-Wagner J, Bremer E. Two evolutionarily closely related ABC transporters mediate the uptake of choline for synthesis of the osmoprotectant glycine betaine in Bacillus subtilis. Mol Microbiol. 1999 Apr;32(1):203-16. PMID:10216873

[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

[3] Du Y, Shi WW, He YX, Yang YH, Zhou CZ, Chen Y. Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC. Biochem J. 2011 Mar 3. PMID:21366542 doi:10.1042/BJ20102097

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
 ==Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC==
-<StructureSection load='3ppn' size='340' side='right' caption='[[3ppn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='3ppn' size='340' side='right'caption='[[3ppn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ppn]] is a 2 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=3PPN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PPN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ppn]] is a 2 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=3PPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PPN FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ppo|3ppo]], [[3ppp|3ppp]], [[3ppq|3ppq]], [[3ppr|3ppr]]</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]] 2.3&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">opuCC ([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'>[https://proteopedia.org/fgij/fg.htm?mol=3ppn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppn OCA], [https://pdbe.org/3ppn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ppn RCSB], [https://www.ebi.ac.uk/pdbsum/3ppn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppn ProSAT]</span></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=3ppn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppn OCA], [http://pdbe.org/3ppn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ppn RCSB], [http://www.ebi.ac.uk/pdbsum/3ppn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/OPUCC_BACSU OPUCC_BACSU]] Member of a high affinity multicomponent binding-protein-dependent transport system for glycine betaine, carnitine, and choline.<ref>PMID:10216873</ref> <ref>PMID:8752321</ref>
+[https://www.uniprot.org/uniprot/OPUCC_BACSU OPUCC_BACSU] Member of a high affinity multicomponent binding-protein-dependent transport system for glycine betaine, carnitine, and choline.<ref>PMID:10216873</ref> <ref>PMID:8752321</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 20: @@
 ==See Also==
-*[[ABC transporter|ABC transporter]]
+*[[ABC transporter 3D structures|ABC transporter 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus globigii migula 1900]]
+[[Category: Bacillus subtilis]]
-[[Category: Chen, Y]]
+[[Category: Large Structures]]
-[[Category: Du, Y]]
+[[Category: Chen Y]]
-[[Category: He, Y X]]
+[[Category: Du Y]]
-[[Category: Shi, W W]]
+[[Category: He YX]]
-[[Category: Yang, Y H]]
+[[Category: Shi WW]]
-[[Category: Zhou, C Z]]
+[[Category: Yang YH]]
-[[Category: Alpha-beta-alpha sandwich]]
+[[Category: Zhou CZ]]
-[[Category: Compatible solute]]
-[[Category: Osmoprotectant]]
-[[Category: Transport protein]]

3ppn: Difference between revisions

Latest revision as of 17:07, 1 November 2023

Structures of the substrate-binding protein provide insights into the multiple compatible solutes binding specificities of Bacillus subtilis ABC transporter OpuC

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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