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.


1evq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1evq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1evq, resolution 2.6&Aring;" /> '''THE CRYSTAL STRUCTURE...)
Current revision (10:06, 20 March 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1evq.gif|left|200px]]<br /><applet load="1evq" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1evq, resolution 2.6&Aring;" />
 
-
'''THE CRYSTAL STRUCTURE OF THE THERMOPHILIC CARBOXYLESTERASE EST2 FROM ALICYCLOBACILLUS ACIDOCALDARIUS'''<br />
 
-
==Overview==
+
==THE CRYSTAL STRUCTURE OF THE THERMOPHILIC CARBOXYLESTERASE EST2 FROM ALICYCLOBACILLUS ACIDOCALDARIUS==
-
EST2 is a novel thermophilic carboxylesterase, isolated and cloned from, Alicyclobacillus (formerly Bacillus) acidocaldarius, which optimally, hydrolyses esters with acyl chain lengths of six to eight carbon atoms at, 70 degrees C. On the basis of the amino acid sequence homology, it has, been classified as a member of the mammalian hormone-sensitive lipase, (HSL) subfamily.The crystal structure of EST2, complexed with a sulphonyl, derivative, has been determined at 2.6 A resolution by a multiple, wavelength anomalous diffraction experiment on a seleno-methionine, derivative. EST2 presents a canonical alpha/beta hydrolase core, shielded, at the C-terminal side by a cap region built up of five helices. It, contains the lipase-like catalytic triad, Ser155, His282 and Asp252, whereby the nucleophile is covalently modified. This allows an unambiguous, view of the putative active site of EST2, detecting the oxyanion hole, in, whose formation the amino acid sequence motif His81-Gly82-Gly83-Gly84 is, involved, and the hydrophobic binding pocket for the acyl chain. The, structural model here reported provides the first example of a transition, state analogue of an esterase/lipase belonging to the HSL group, thus, affording useful information for the design of medical inhibitors., Moreover, as the first X-ray structure of a thermophilic carboxylesterase, the comparison with its mesophilic homologue, the Brefeldin A esterase, (BFAE) from Bacillus subtilis, allows the identification of putative, determinants of thermal stability.
+
<StructureSection load='1evq' size='340' side='right'caption='[[1evq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1evq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EVQ FirstGlance]. <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]] 2.6&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=1evq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1evq OCA], [https://pdbe.org/1evq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1evq RCSB], [https://www.ebi.ac.uk/pdbsum/1evq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1evq ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q7SIG1_ALIAC Q7SIG1_ALIAC]
 +
== 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/ev/1evq_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=1evq ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1EVQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius] with EPE and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EVQ OCA].
+
*[[Lipase 3D Structures|Lipase 3D Structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
A snapshot of a transition state analogue of a novel thermophilic esterase belonging to the subfamily of mammalian hormone-sensitive lipase., De Simone G, Galdiero S, Manco G, Lang D, Rossi M, Pedone C, J Mol Biol. 2000 Nov 10;303(5):761-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11061974 11061974]
+
[[Category: Alicyclobacillus acidocaldarius]]
[[Category: Alicyclobacillus acidocaldarius]]
-
[[Category: Carboxylesterase]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: De Simone G]]
-
[[Category: Galdiero, S.]]
+
[[Category: Galdiero S]]
-
[[Category: Lang, D.]]
+
[[Category: Lang D]]
-
[[Category: Manco, G.]]
+
[[Category: Manco G]]
-
[[Category: Pedone, C.]]
+
[[Category: Pedone C]]
-
[[Category: Rossi, M.]]
+
[[Category: Rossi M]]
-
[[Category: Simone, G.De.]]
+
-
[[Category: EPE]]
+
-
[[Category: TRS]]
+
-
[[Category: alpha/beta hydrolase fold]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:54:31 2007''
+

Current revision

THE CRYSTAL STRUCTURE OF THE THERMOPHILIC CARBOXYLESTERASE EST2 FROM ALICYCLOBACILLUS ACIDOCALDARIUS

PDB ID 1evq

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/1evq"
Personal tools