View source for 5g5c


==Structure of the Pyrococcus furiosus Esterase Pf2001 with space group C2221==
<StructureSection load='5g5c' size='340' side='right' caption='[[5g5c]], [[Resolution|resolution]] 1.18&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5g5c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G5C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5G5C FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5g59|5g59]], [[5g5m|5g5m]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5g5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g5c OCA], [http://pdbe.org/5g5c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g5c RCSB], [http://www.ebi.ac.uk/pdbsum/5g5c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g5c ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Lipases and esterases constitute a group of enzymes that catalyze the hydrolysis or synthesis of ester bonds. A major biotechnological interest corresponds to thermophilic esterases, due to their intrinsic stability at high temperatures. The Pf2001 esterase from Pyrococcus furiosus reaches its optimal activity between 70 degrees C and 80 degrees C. The crystal structure of the Pf2001 esterase shows two different conformations: monomer and dimer. The structures reveal important rearrangements in the "cap" subdomain between monomer and dimer, by the formation of an extensive intertwined helical interface. Moreover, the dimer interface is essential for the formation of the hydrophobic channel for substrate selectivity, as confirmed by mutagenesis and kinetic analysis. We also provide evidence for dimer formation at high temperatures, a process that correlates with its enzymatic activation. Thus, we propose a temperature-dependent activation mechanism of the Pf2001 esterase via dimerization that is necessary for the substrate channel formation in the active-site cleft.

Structural Mechanism for the Temperature-Dependent Activation of the Hyperthermophilic Pf2001 Esterase.,Varejao N, De-Andrade RA, Almeida RV, Anobom CD, Foguel D, Reverter D Structure. 2017 Dec 28. pii: S0969-2126(17)30403-3. doi:, 10.1016/j.str.2017.12.004. PMID:29307486<ref>PMID:29307486</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5g5c" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Atcc 43587]]
[[Category: Reverter, D]]
[[Category: Varejao, N]]
[[Category: Esterase]]
[[Category: Structural protein]]
[[Category: Themophilic]]