4cg3: Difference between revisions

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-'''Unreleased structure'''
+==Structural and functional studies on a thermostable polyethylene therephtalate degrading hydrolase from Thermobifida fusca==
+<StructureSection load='4cg3' size='340' side='right' caption='[[4cg3]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4cg3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CG3 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cg1|4cg1]], [[4cg2|4cg2]]</td></tr>
+<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cutinase Cutinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.74 3.1.1.74] </span></td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4cg3 PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Bacterial cutinases are promising catalysts for the modification and degradation of the widely used plastic polyethylene terephthalate (PET). The improvement of the enzyme for industrial purposes is limited due to the lack of structural information for cutinases of bacterial origin. We have crystallized and structurally characterized a cutinase from Thermobifida fusca KW3 (TfCut2) in free as well as in inhibitor-bound form. Together with our analysis of the thermal stability and modelling studies, we suggest possible reasons for the outstanding thermostability in comparison to the less thermostable homolog from Thermobifida alba AHK119 and propose a model for the binding of the enzyme towards its polymeric substrate. The TfCut2 structure is the basis for the rational design of catalytically more efficient enzyme variants for the hydrolysis of PET and other synthetic polyesters.
-The entry 4cg3 is ON HOLD  until Paper Publication
+Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca.,Roth C, Wei R, Oeser T, Then J, Follner C, Zimmermann W, Strater N Appl Microbiol Biotechnol. 2014 Apr 13. PMID:24728714<ref>PMID:24728714</ref>
-Authors: Roth, C., Wei, R., Oeser, T., Then, J., Foellner, C., Zimmermann, W., Straeter, N.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Structural and functional studies on a thermostable polyethylene therephtalate degrading hydrolase from Thermobifida fusca
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Cutinase]]
+[[Category: Foellner, C.]]
+[[Category: Oeser, T.]]
+[[Category: Roth, C.]]
+[[Category: Straeter, N.]]
+[[Category: Then, J.]]
+[[Category: Wei, R.]]
+[[Category: Zimmermann, W.]]
+[[Category: Alpha-beta- fold]]
+[[Category: Hydrolase]]
+[[Category: Pet degradation]]