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| | ==Crystal structure of sshesti PE mutant== | | ==Crystal structure of sshesti PE mutant== |
| - | <StructureSection load='4p9n' size='340' side='right' caption='[[4p9n]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='4p9n' size='340' side='right'caption='[[4p9n]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4p9n]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P9N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P9N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4p9n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_shibatae Saccharolobus shibatae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P9N FirstGlance]. <br> |
| - | </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=4p9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p9n OCA], [http://pdbe.org/4p9n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p9n RCSB], [http://www.ebi.ac.uk/pdbsum/4p9n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p9n ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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=4p9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p9n OCA], [https://pdbe.org/4p9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p9n RCSB], [https://www.ebi.ac.uk/pdbsum/4p9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p9n ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5NU42_9CREN Q5NU42_9CREN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Carboxylesterase|Carboxylesterase]] | + | *[[Carboxylesterase 3D structures|Carboxylesterase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Unno, H]] | + | [[Category: Large Structures]] |
| - | [[Category: Alpha/beta-hydrorase fold]] | + | [[Category: Saccharolobus shibatae]] |
| - | [[Category: Carboxylesterase]] | + | [[Category: Unno H]] |
| - | [[Category: Hydrolase]]
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| Structural highlights
Function
Q5NU42_9CREN
Publication Abstract from PubMed
To investigate the mechanism for low-pH adaptation by a carboxylesterase, structural and biochemical analyses of EstFa_R (a recombinant, slightly acidophilic carboxylesterase from Ferroplasma acidiphilum) and SshEstI (an alkaliphilic carboxylesterase from Sulfolobus shibatae DSM5389) were performed. Although a previous proteomic study by another group showed that the enzyme purified from F. acidiphilum contained an iron atom, EstFa_R did not bind to iron, as analyzed by ICP-MS and isothermal titration calorimetry. The crystal structures of EstFa_R and SshEstI were determined at 1.6A and 1.5A resolutions, respectively. EstFa_R had a catalytic triad with an extended hydrogen bond network that was not observed in SshEstI. Quadruple mutants of both proteins were created to remove or introduce the extended hydrogen bond network. The mutation on EstFa_R enhanced its catalytic efficiency and gave it an alkaline pH optimum, whereas the mutation on SshEstI resulted in opposite effects (i.e., decrease in the catalytic efficiency and a downward shift in the optimum pH). Our experimental results suggest that the low pH optimum of EstFa_R activity was a result of the unique extended hydrogen bond network in the catalytic triad and the highly negative charged surface around the active site. The change in the pH optimum of EstFa_R happened simultaneously with a change in the catalytic efficiency, suggesting that the local flexibility of the active site in EstFa_R could be modified by quadruple mutation. These observations may provide a novel strategy to elucidate the low-pH adaptation of serine hydrolases.
Structural Insights into the Low-pH Adaptation of a Unique Carboxylesterase from Ferroplasma: Altering the pH Optima of Two Carboxylesterases.,Ohara K, Unno H, Oshima Y, Hosoya M, Fujino N, Hirooka K, Takahashi S, Yamashita S, Kusunoki M, Nakayama T J Biol Chem. 2014 Jul 20. pii: jbc.M113.521856. PMID:25043762[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ohara K, Unno H, Oshima Y, Hosoya M, Fujino N, Hirooka K, Takahashi S, Yamashita S, Kusunoki M, Nakayama T. Structural Insights into the Low-pH Adaptation of a Unique Carboxylesterase from Ferroplasma: Altering the pH Optima of Two Carboxylesterases. J Biol Chem. 2014 Jul 20. pii: jbc.M113.521856. PMID:25043762 doi:http://dx.doi.org/10.1074/jbc.M113.521856
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