This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1tqh

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:15, 12 October 2017

Covalent Reaction intermediate Revealed in Crystal Structure of the Geobacillus stearothermophilus Carboxylesterase Est30

Structural highlights

1tqh is a 1 chain structure with sequence from Atcc 12980. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Carboxylesterase, with EC number 3.1.1.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[EST_GEOSE] Involved in the detoxification of xenobiotics. Shows maximal activity with C6 substrates, with gradually decreasing activity from C8 to C12 substrates. No activity for higher chain length substrates acids rather than long-chain ones.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Est30 is a thermophilic carboxylesterase cloned from Geobacillus stearothermophilus that showed optimal hydrolysis of esters with short acyl chains at 70 degrees C. Est30 is a member of a new family of carboxylesterases with representatives in other Gram-positive bacteria. The crystal structure has been determined at 1.63A resolution using multiple anomalous dispersion data. The two-domain crystal structure showed a large domain with a modified alpha/beta hydrolase core including a seven, rather than an eight-stranded beta sheet, and a smaller cap domain comprising three alpha helices. The catalytic triad consists of residues Ser94, Asp193, and His223. A 100Da tetrahedral ligand was observed to be covalently bound to the side-chain of Ser94. The propyl acetate ligand represents the first tetrahedral intermediate in the reaction mechanism. Therefore, this Est30 crystal structure will help understand the mode of action of all enzymes in the serine hydrolase superfamily.

Covalent reaction intermediate revealed in crystal structure of the Geobacillus stearothermophilus carboxylesterase Est30.,Liu P, Wang YF, Ewis HE, Abdelal AT, Lu CD, Harrison RW, Weber IT J Mol Biol. 2004 Sep 10;342(2):551-61. PMID:15327954^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Liu P, Wang YF, Ewis HE, Abdelal AT, Lu CD, Harrison RW, Weber IT. Covalent reaction intermediate revealed in crystal structure of the Geobacillus stearothermophilus carboxylesterase Est30. J Mol Biol. 2004 Sep 10;342(2):551-61. PMID:15327954 doi:10.1016/j.jmb.2004.06.069

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tqh"

@@ Line 1: / Line 1: @@
 ==Covalent Reaction intermediate Revealed in Crystal Structure of the Geobacillus stearothermophilus Carboxylesterase Est30==
 <StructureSection load='1tqh' size='340' side='right' caption='[[1tqh]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4PA:PROPYL+ACETATE'>4PA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </span></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=1tqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tqh OCA], [http://pdbe.org/1tqh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tqh RCSB], [http://www.ebi.ac.uk/pdbsum/1tqh PDBsum]</span></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=1tqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tqh OCA], [http://pdbe.org/1tqh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tqh RCSB], [http://www.ebi.ac.uk/pdbsum/1tqh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tqh ProSAT]</span></td></tr>
 </table>
 == Function ==

1tqh

From Proteopedia

Revision as of 10:15, 12 October 2017

Covalent Reaction intermediate Revealed in Crystal Structure of the Geobacillus stearothermophilus Carboxylesterase Est30

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox