3klk: Difference between revisions

<table><tr><td colspan='2'>[[3klk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_23272 Atcc 23272]. The June 2011 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Glucansucrase''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2011_6 10.2210/rcsb_pdb/mom_2011_6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KLK 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=GOL:GLYCEROL'>GOL</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;'>[[3hq3|3hq3]], [[3hz3|3hz3]], [[3kll|3kll]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gtf180 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1598 ATCC 23272])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dextransucrase Dextransucrase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.5 2.4.1.5] </span></td></tr>

== Publication Abstract from PubMed ==

Glucansucrases are large enzymes belonging to glycoside hydrolase family 70, which catalyze the cleavage of sucrose into fructose and glucose, with the concomitant transfer of the glucose residue to a growing alpha-glucan polymer. Among others, plaque-forming oral bacteria secrete these enzymes to produce alpha-glucans, which facilitate the adhesion of the bacteria to the tooth enamel. We determined the crystal structure of a fully active, 1,031-residue fragment encompassing the catalytic and C-terminal domains of GTF180 from Lactobacillus reuteri 180, both in the native state, and in complexes with sucrose and maltose. These structures show that the enzyme has an alpha-amylase-like (beta/alpha)(8)-barrel catalytic domain that is circularly permuted compared to the catalytic domains of members of glycoside hydrolase families 13 and 77, which belong to the same GH-H superfamily. In contrast to previous suggestions, the enzyme has only one active site and one nucleophilic residue. Surprisingly, in GTF180 the peptide chain follows a "U"-path, such that four of the five domains are made up from discontiguous N- and C-terminal stretches of the peptide chain. Finally, the structures give insight into the factors that determine the different linkage types in the polymeric product.

 

Crystal structure of a 117 kDa glucansucrase fragment provides insight into evolution and product specificity of GH70 enzymes.,Vujicic-Zagar A, Pijning T, Kralj S, Lopez CA, Eeuwema W, Dijkhuizen L, Dijkstra BW Proc Natl Acad Sci U S A. 2010 Nov 30. PMID:21118988<ref>PMID:21118988</ref>

 

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

<div class="pdbe-citations 3klk" style="background-color:#fffaf0;"></div>

[[Category: Dijkhuizen, L]]

[[Category: Dijkstra, B W]]

[[Category: Eeuwema, W]]

[[Category: Kralj, S]]

[[Category: Pijning, T]]

[[Category: Vujicic-Zagar, A]]

[[Category: Transferase]]