3kof: Difference between revisions

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-{{Seed}}
-[[Image:3kof.png|left|200px]]
-<!--
+==Crystal structure of the double mutant F178Y/R181E of E.coli transaldolase B==
-The line below this paragraph, containing "STRUCTURE_3kof", creates the "Structure Box" on the page.
+<StructureSection load='3kof' size='340' side='right'caption='[[3kof]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3kof]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KOF FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_3kof|  PDB=3kof  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3kof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kof OCA], [https://pdbe.org/3kof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kof RCSB], [https://www.ebi.ac.uk/pdbsum/3kof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kof ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TALB_ECOLI TALB_ECOLI] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.[HAMAP-Rule:MF_00492]
+== 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/ko/3kof_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=3kof ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Recently, we reported on a transaldolase B variant (TalB F178Y) that is able to use dihydroxyacetone (DHA) as donor in aldol reactions. In a second round of protein engineering, we aimed at improving the affinity of this variant towards nonphosphorylated acceptor aldehydes, that is, glyceraldehyde (GA). The anion binding site was identified in the X-ray structure of TalB F178Y where a sulfate ion from the buffer was bound in the active site. Therefore, we performed site-directed saturation mutagenesis at three residues forming the putative phosphate binding site, Arg181, Ser226 and Arg228. The focused libraries were screened for the formation of D-fructose from DHA and d,l-GA by using an adjusted colour assay. The best results with respect to the synthesis of D-fructose were achieved with the TalB F178Y/R181E variant, which exhibited an at least fivefold increase in affinity towards d,l-GA (K(M)=24 mM). We demonstrated that this double mutant can use D-GA, glycolaldehyde and the L-isomer, L-GA, as acceptor substrates. This resulted in preparative synthesis of D-fructose, D-xylulose and L-sorbose when DHA was used as donor. Hence, we engineered a DHA-dependent aldolase that can synthesise the formation of polyhydroxylated compounds from simple and cheap substrates at preparative scale.
-===Crystal structure of the double mutant F178Y/R181E of E.coli transaldolase B===
+Redesigning the Active Site of Transaldolase TalB from Escherichia coli: New Variants with Improved Affinity towards Nonphosphorylated Substrates.,Schneider S, Gutierrez M, Sandalova T, Schneider G, Clapes P, Sprenger GA, Samland AK Chembiochem. 2010 Feb 10. PMID:20148428<ref>PMID:20148428</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3kof" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_20148428}}, adds the Publication Abstract to the page
+*[[Transaldolase 3D structures|Transaldolase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 20148428 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_20148428}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Escherichia coli K-12]]
-KOF is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KOF OCA].
+[[Category: Large Structures]]
+[[Category: Clapes P]]
-==Reference==
+[[Category: Gutierrez M]]
-<ref group="xtra">PMID:20148428</ref><references group="xtra"/>
+[[Category: Samland AK]]
-[[Category: Escherichia coli k-12]]
+[[Category: Sandalova T]]
-[[Category: Transaldolase]]
+[[Category: Schneider G]]
-[[Category: Clapes, P.]]
+[[Category: Schneider S]]
-[[Category: Gutierrez, M.]]
+[[Category: Sprenger GA]]
-[[Category: Samland, A K.]]
-[[Category: Sandalova, T.]]
-[[Category: Schneider, G.]]
-[[Category: Schneider, S.]]
-[[Category: Sprenger, G A.]]
-[[Category: Aldolase]]
-[[Category: Cytoplasm]]
-[[Category: Directed evolution]]
-[[Category: Pentose shunt]]
-[[Category: Transaldolase]]
-[[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 14 09:06:04 2010''