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3oo9

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Current revision (11:17, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3oo9' size='340' side='right'caption='[[3oo9]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
<StructureSection load='3oo9' size='340' side='right'caption='[[3oo9]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3oo9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acts5 Acts5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OO9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3oo9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinoplanes_sp._SE50/110 Actinoplanes sp. SE50/110]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OO9 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3oo6|3oo6]], [[3oo7|3oo7]], [[3oo8|3oo8]], [[3ooa|3ooa]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AcbH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=134676 ACTS5])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oo9 OCA], [https://pdbe.org/3oo9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oo9 RCSB], [https://www.ebi.ac.uk/pdbsum/3oo9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oo9 ProSAT]</span></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=3oo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oo9 OCA], [https://pdbe.org/3oo9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oo9 RCSB], [https://www.ebi.ac.uk/pdbsum/3oo9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oo9 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q27GR2_ACTS5 Q27GR2_ACTS5]
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Solute receptors (binding proteins) are indispensable components of canonical ATP-binding cassette importers in prokaryotes. Here, we report on the characterization and crystal structures in the closed and open conformations of AcbH, the solute receptor of the putative carbohydrate transporter AcbFG which is encoded in the acarbose (acarviosyl-1,4-maltose) biosynthetic gene cluster from Actinoplanes sp. SE50/110. Binding assays identified AcbH as a high-affinity monosaccharide-binding protein with a dissociation constant (K(d)) for beta-d-galactopyranose of 9.8+/-1.0 nM. Neither galactose-containing di- and trisaccharides, such as lactose and raffinose, nor monosaccharides including d-galacturonic acid, l-arabinose, d-xylose and l-rhamnose competed with [(1)(4)C]galactose for binding to AcbH. Moreover, AcbH does not bind d-glucose, which is a common property of all but one d-galactose-binding proteins characterized to date. Strikingly, determination of the X-ray structure revealed that AcbH is structurally homologous to maltose-binding proteins rather than to glucose-binding proteins. Two helices are inserted in the substrate-binding pocket, which reduces the cavity size and allows the exclusive binding of monosaccharides, specifically beta-d-galactopyranose, in the (4)C(1) conformation. Site-directed mutagenesis of three residues from the binding pocket (Arg82, Asp361 and Arg362) that interact with the axially oriented O4-H hydroxyl of the bound galactopyranose and subsequent functional analysis indicated that these residues are crucial for galactose binding. To our knowledge, this is the first report of the tertiary structure of a solute receptor with exclusive affinity for beta-d-galactopyranose. The putative role of a galactose import system in the context of acarbose metabolism in Actinoplanes sp. is discussed.
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Crystal structures of the bacterial solute receptor AcbH displaying an exclusive substrate preference for beta-D-galactopyranose.,Licht A, Bulut H, Scheffel F, Daumke O, Wehmeier UF, Saenger W, Schneider E, Vahedi-Faridi A J Mol Biol. 2011 Feb 11;406(1):92-105. Epub 2010 Dec 17. PMID:21168419<ref>PMID:21168419</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3oo9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acts5]]
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[[Category: Actinoplanes sp. SE50/110]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bulut, H]]
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[[Category: Bulut H]]
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[[Category: Licht, A]]
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[[Category: Licht A]]
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[[Category: Vahedi-Faridi, A]]
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[[Category: Vahedi-Faridi A]]
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[[Category: Abc transporter extracellular solute binding protein]]
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[[Category: Class 2 sbp fold]]
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[[Category: D-galactose binding]]
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[[Category: Sugar binding protein]]
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Current revision

Crystal structures and biochemical characterization of the bacterial solute receptor AcbH reveal an unprecedented exclusive substrate preference for b-D-galactopyranose

PDB ID 3oo9

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