3ls2: Difference between revisions
No edit summary |
No edit summary |
||
| (7 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of an S-formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125== | |||
<StructureSection load='3ls2' size='340' side='right'caption='[[3ls2]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ls2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoalteromonas_translucida_TAC125 Pseudoalteromonas translucida TAC125]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LS2 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]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=3ls2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ls2 OCA], [https://pdbe.org/3ls2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ls2 RCSB], [https://www.ebi.ac.uk/pdbsum/3ls2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ls2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q3IL66_PSET1 Q3IL66_PSET1] Serine hydrolase involved in the detoxification of formaldehyde.[RuleBase:RU363068] | |||
== 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/ls/3ls2_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=3ls2 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
S-formylglutathione hydrolases (FGHs) constitute a family of ubiquitous enzymes which play a key role in formaldehyde detoxification both in prokaryotes and eukaryotes, catalyzing the hydrolysis of S-formylglutathione to formic acid and glutathione. While a large number of functional studies have been reported on these enzymes, few structural studies have so far been carried out. In this paper we report on the functional and structural characterization of PhEst, a FGH isolated from the psychrophilic bacterium Pseudoalteromonas haloplanktis. According to our functional studies, this enzyme is able to efficiently hydrolyze several thioester substrates with very small acyl moieties. By contrast, the enzyme shows no activity toward substrates with bulky acyl groups. These data are in line with structural studies which highlight for this enzyme a very narrow acyl-binding pocket in a typical alpha/beta-hydrolase fold. PhEst represents the first cold-adapted FGH structurally characterized to date; comparison with its mesophilic counterparts of known three-dimensional structure allowed to obtain useful insights into molecular determinants responsible for the ability of this psychrophilic enzyme to work at low temperature. (c) 2010 Wiley Periodicals, Inc. Biopolymers, 2010. | |||
Crystal structure of an S-formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125.,Alterio V, Aurilia V, Romanelli A, Parracino A, Saviano M, D'Auria S, De Simone G Biopolymers. 2010 Mar 5. PMID:20209484<ref>PMID:20209484</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3ls2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudoalteromonas translucida TAC125]] | |||
[[Category: Alterio V]] | |||
[[Category: De Simone G]] | |||
Latest revision as of 11:43, 6 September 2023
Crystal structure of an S-formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125Crystal structure of an S-formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125
Structural highlights
FunctionQ3IL66_PSET1 Serine hydrolase involved in the detoxification of formaldehyde.[RuleBase:RU363068] 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 PubMedS-formylglutathione hydrolases (FGHs) constitute a family of ubiquitous enzymes which play a key role in formaldehyde detoxification both in prokaryotes and eukaryotes, catalyzing the hydrolysis of S-formylglutathione to formic acid and glutathione. While a large number of functional studies have been reported on these enzymes, few structural studies have so far been carried out. In this paper we report on the functional and structural characterization of PhEst, a FGH isolated from the psychrophilic bacterium Pseudoalteromonas haloplanktis. According to our functional studies, this enzyme is able to efficiently hydrolyze several thioester substrates with very small acyl moieties. By contrast, the enzyme shows no activity toward substrates with bulky acyl groups. These data are in line with structural studies which highlight for this enzyme a very narrow acyl-binding pocket in a typical alpha/beta-hydrolase fold. PhEst represents the first cold-adapted FGH structurally characterized to date; comparison with its mesophilic counterparts of known three-dimensional structure allowed to obtain useful insights into molecular determinants responsible for the ability of this psychrophilic enzyme to work at low temperature. (c) 2010 Wiley Periodicals, Inc. Biopolymers, 2010. Crystal structure of an S-formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125.,Alterio V, Aurilia V, Romanelli A, Parracino A, Saviano M, D'Auria S, De Simone G Biopolymers. 2010 Mar 5. PMID:20209484[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||