View source for 1ufa


==Crystal structure of TT1467 from Thermus thermophilus HB8==
<StructureSection load='1ufa' size='340' side='right'caption='[[1ufa]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ufa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UFA FirstGlance]. <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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1ufa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ufa OCA], [https://pdbe.org/1ufa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ufa RCSB], [https://www.ebi.ac.uk/pdbsum/1ufa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ufa ProSAT], [https://www.topsan.org/Proteins/RSGI/1ufa TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BE_THET8 BE_THET8] Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 3 to 13, with two local maxima at DP 7 and DP 11. Exhibits an alpha-retaining catalytic mechanism. Is involved in glycogen biosynthesis. Shows a secondary activity, i.e. the hydrolysis of the substrate, being 4% of the total activity. Can use amylose as substrate but not alpha-1,4-linked oligosaccharides of 2-7 glucose residues, beta-cyclodextrin, 6-O-glucosyl-beta-cyclodextrin and 6-O-maltosyl-beta-cyclodextrin. Is not able to branch amylopectin further, it only hydrolyzes amylopectin. Thus, displays preference for linear and long substrates (amylose) over branched structures (amylopectin).<ref>PMID:21097495</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/uf/1ufa_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ufa ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus]]
[[Category: Idaka M]]
[[Category: Ishitani R]]
[[Category: Kuramitsu S]]
[[Category: Murayama K]]
[[Category: Nureki O]]
[[Category: Shirouzu M]]
[[Category: Terada T]]
[[Category: Yamaguchi H]]
[[Category: Yokoyama S]]