3ls2: Difference between revisions
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==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 [http://en.wikipedia.org/wiki/Pseudoalteromonas_haloplanktis Pseudoalteromonas haloplanktis]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LS2 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PSHAa1385 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=228 Pseudoalteromonas haloplanktis])</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=3ls2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ls2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ls2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ls2 PDBsum]</span></td></tr> | |||
</table> | |||
== 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/chain_selection.php?pdb_ID=2ata 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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Pseudoalteromonas haloplanktis]] | [[Category: Pseudoalteromonas haloplanktis]] | ||
[[Category: Alterio, V | [[Category: Alterio, V]] | ||
[[Category: Simone, G De | [[Category: Simone, G De]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Pseudoalteromonas haloplankti]] | [[Category: Pseudoalteromonas haloplankti]] | ||
[[Category: Psychrophilic organism]] | [[Category: Psychrophilic organism]] | ||
[[Category: S-formylglutathione hydrolase]] | [[Category: S-formylglutathione hydrolase]] | ||
Revision as of 18:18, 18 December 2014
Crystal structure of an S-formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125Crystal structure of an S-formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125
Structural highlights
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
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