4cg1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (02:44, 21 November 2024) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca==
==Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca==
-
<StructureSection load='4cg1' size='340' side='right' caption='[[4cg1]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
+
<StructureSection load='4cg1' size='340' side='right'caption='[[4cg1]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4cg1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CG1 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4cg1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CG1 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>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
-
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cg2|4cg2]], [[4cg3|4cg3]]</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>
-
<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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg1 OCA], [https://pdbe.org/4cg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cg1 RCSB], [https://www.ebi.ac.uk/pdbsum/4cg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cg1 ProSAT]</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=4cg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cg1 RCSB], [http://www.ebi.ac.uk/pdbsum/4cg1 PDBsum]</span></td></tr>
+
</table>
-
<table>
+
== Function ==
 +
[https://www.uniprot.org/uniprot/PETH2_THEFU PETH2_THEFU] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:23604968, PubMed:24728714, PubMed:31690819, Ref.4). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:15638529, PubMed:23604968, PubMed:24728714, PubMed:25545638, PubMed:31690819, Ref.4). Also hydrolyzes the triglycerides triacetin, tributyrin, tricaprin, and trilaurin, with a preference for short-chain substrates (PubMed:15638529). Hydrolyzes the hemicellulose xylan (PubMed:20816933). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (PubMed:25545638, PubMed:31690819, PubMed:32269349, Ref.4). Can also depolymerize poly(epsilon-caprolactone) (PCL), a synthetic aliphatic biodegradable polyester (PubMed:15638529). Hydrolyzes polyoxyethylenesorbate esters with a preference for shorter chain lengths (PubMed:20816933).<ref>PMID:15638529</ref> <ref>PMID:20816933</ref> <ref>PMID:23604968</ref> <ref>PMID:24728714</ref> <ref>PMID:25545638</ref> <ref>PMID:31690819</ref> <ref>PMID:32269349</ref> <ref>PMID:20816933</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 16: Line 18:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
 +
<div class="pdbe-citations 4cg1" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Cutinase 3D structures|Cutinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Cutinase]]
+
[[Category: Large Structures]]
-
[[Category: Foellner, C.]]
+
[[Category: Thermobifida fusca]]
-
[[Category: Oeser, T.]]
+
[[Category: Foellner C]]
-
[[Category: Roth, C.]]
+
[[Category: Oeser T]]
-
[[Category: Straeter, N.]]
+
[[Category: Roth C]]
-
[[Category: Then, J.]]
+
[[Category: Straeter N]]
-
[[Category: Wei, R.]]
+
[[Category: Then J]]
-
[[Category: Zimmermann, W.]]
+
[[Category: Wei R]]
-
[[Category: Alpha beta fold]]
+
[[Category: Zimmermann W]]
-
[[Category: Hydrolase]]
+
-
[[Category: Pet degradation]]
+

Current revision

Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca

PDB ID 4cg1

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4cg1"
Personal tools