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< | ==Crystal structure of psychrotrophic esterase EstA from Pseudoalteromonas sp. 643A inhibited by monoethylphosphonate== | ||
<StructureSection load='3hp4' size='340' side='right'caption='[[3hp4]], [[Resolution|resolution]] 1.35Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3hp4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoalteromonas_sp._643A Pseudoalteromonas sp. 643A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HP4 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]] 1.35Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MIR:MONOETHYLPHOSPHORYLSERINE'>MIR</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=3hp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hp4 OCA], [https://pdbe.org/3hp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hp4 RCSB], [https://www.ebi.ac.uk/pdbsum/3hp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hp4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q1G1I7_9GAMM Q1G1I7_9GAMM] | |||
== 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/hp/3hp4_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=3hp4 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of the esterase EstA from the cold-adapted bacterium Pseudoalteromonas sp. 643A was determined in a covalently inhibited form at a resolution of 1.35 A. The enzyme has a typical SGNH hydrolase structure consisting of a single domain containing a five-stranded beta-sheet, with three helices at the convex side and two helices at the concave side of the sheet, and is ornamented with a couple of very short helices at the domain edges. The active site is located in a groove and contains the classic catalytic triad of Ser, His and Asp. In the structure of the crystal soaked in diethyl p-nitrophenyl phosphate (DNP), the catalytic serine is covalently connected to a phosphonate moiety that clearly has only one ethyl group. This is the only example in the Protein Data Bank of a DNP-inhibited enzyme with covalently bound monoethylphosphate. | |||
Structure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonate.,Brzuszkiewicz A, Nowak E, Dauter Z, Dauter M, Cieslinski H, Dlugolecka A, Kur J Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Sep 1;65(Pt, 9):862-5. Epub 2009 Aug 20. PMID:19724118<ref>PMID:19724118</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3hp4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: Pseudoalteromonas sp. 643A]] | |||
[[Category: Brzuszkiewicz A]] | |||
== | [[Category: Cieslinski H]] | ||
< | [[Category: Dauter M]] | ||
[[Category: Pseudoalteromonas sp. | [[Category: Dauter Z]] | ||
[[Category: Brzuszkiewicz | [[Category: Kur J]] | ||
[[Category: Cieslinski | [[Category: Nowak E]] | ||
[[Category: Dauter | |||
[[Category: Dauter | |||
[[Category: Kur | |||
[[Category: Nowak | |||
Latest revision as of 10:25, 6 September 2023
Crystal structure of psychrotrophic esterase EstA from Pseudoalteromonas sp. 643A inhibited by monoethylphosphonateCrystal structure of psychrotrophic esterase EstA from Pseudoalteromonas sp. 643A inhibited by monoethylphosphonate
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of the esterase EstA from the cold-adapted bacterium Pseudoalteromonas sp. 643A was determined in a covalently inhibited form at a resolution of 1.35 A. The enzyme has a typical SGNH hydrolase structure consisting of a single domain containing a five-stranded beta-sheet, with three helices at the convex side and two helices at the concave side of the sheet, and is ornamented with a couple of very short helices at the domain edges. The active site is located in a groove and contains the classic catalytic triad of Ser, His and Asp. In the structure of the crystal soaked in diethyl p-nitrophenyl phosphate (DNP), the catalytic serine is covalently connected to a phosphonate moiety that clearly has only one ethyl group. This is the only example in the Protein Data Bank of a DNP-inhibited enzyme with covalently bound monoethylphosphate. Structure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonate.,Brzuszkiewicz A, Nowak E, Dauter Z, Dauter M, Cieslinski H, Dlugolecka A, Kur J Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Sep 1;65(Pt, 9):862-5. Epub 2009 Aug 20. PMID:19724118[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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