View source for 3ckc


==B. thetaiotaomicron SusD==
<StructureSection load='3ckc' size='340' side='right'caption='[[3ckc]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ckc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bactn Bactn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CKC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ck7|3ck7]], [[3ck8|3ck8]], [[3ck9|3ck9]], [[3ckb|3ckb]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SusD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=226186 BACTN])</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=3ckc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ckc OCA], [https://pdbe.org/3ckc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ckc RCSB], [https://www.ebi.ac.uk/pdbsum/3ckc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ckc ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/SUSD_BACTN SUSD_BACTN]] Major starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation.<ref>PMID:10986238</ref> <ref>PMID:11717282</ref> <ref>PMID:18611383</ref> <ref>PMID:9006015</ref>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ck/3ckc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=3ckc ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
The human gut microbiota performs functions that are not encoded in our Homo sapiens genome, including the processing of otherwise undigestible dietary polysaccharides. Defining the structures of proteins involved in the import and degradation of specific glycans by saccharolytic bacteria complements genomic analysis of the nutrient-processing capabilities of gut communities. Here, we describe the atomic structure of one such protein, SusD, required for starch binding and utilization by Bacteroides thetaiotaomicron, a prominent adaptive forager of glycans in the distal human gut microbiota. The binding pocket of this unique alpha-helical protein contains an arc of aromatic residues that complements the natural helical structure of starch and imposes this conformation on bound maltoheptaose. Furthermore, SusD binds cyclic oligosaccharides with higher affinity than linear forms. The structures of several SusD/oligosaccharide complexes reveal an inherent ligand recognition plasticity dominated by the three-dimensional conformation of the oligosaccharides rather than specific interactions with the composite sugars.

Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices.,Koropatkin NM, Martens EC, Gordon JI, Smith TJ Structure. 2008 Jul;16(7):1105-15. PMID:18611383<ref>PMID:18611383</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3ckc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bactn]]
[[Category: Large Structures]]
[[Category: Gordon, J I]]
[[Category: Koropatkin, N M]]
[[Category: Martens, E C]]
[[Category: Smith, T J]]
[[Category: Carbohydrate binding]]
[[Category: Starch binding]]
[[Category: Sugar binding protein]]
[[Category: Tpr repeat]]