3p0b
From Proteopedia
(Difference between revisions)
| (5 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | {{STRUCTURE_3p0b| PDB=3p0b | SCENE= }} | ||
| - | ===Thermus thermophilus family GH57 branching enzyme: crystal structure, mechanism of action and products formed=== | ||
| - | {{ABSTRACT_PUBMED_021097495}} | ||
| - | == | + | ==Thermus thermophilus family GH57 branching enzyme: crystal structure, mechanism of action and products formed== |
| - | [[http://www.uniprot.org/uniprot/ | + | <StructureSection load='3p0b' size='340' side='right'caption='[[3p0b]], [[Resolution|resolution]] 1.35Å' scene=''> |
| - | + | == Structural highlights == | |
| - | == | + | <table><tr><td colspan='2'>[[3p0b]] 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=3P0B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P0B 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]] 1.35Å</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></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=3p0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p0b OCA], [https://pdbe.org/3p0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p0b RCSB], [https://www.ebi.ac.uk/pdbsum/3p0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p0b ProSAT]</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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
| - | [[Category: Dijkstra | + | [[Category: Dijkstra BW]] |
| - | [[Category: Pijning | + | [[Category: Pijning T]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Thermus thermophilus family GH57 branching enzyme: crystal structure, mechanism of action and products formed
| |||||||||||
