7qop: Difference between revisions

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'''Unreleased structure'''


The entry 7qop is ON HOLD  until Paper Publication
==A mutant of the nitrile hydratase from Geobacillus pallidus having enhanced thermostability==
<StructureSection load='7qop' size='340' side='right'caption='[[7qop]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7qop]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeribacillus_pallidus Aeribacillus pallidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QOP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QOP 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]] 1.8&#8491;</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>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7qop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qop OCA], [https://pdbe.org/7qop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qop RCSB], [https://www.ebi.ac.uk/pdbsum/7qop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qop ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q84FS5_9BACI Q84FS5_9BACI]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nitrile hydratases (NHases) are important biocatalysts for the enzymatic conversion of nitriles to industrially-important amides such as acrylamide and nicotinamide. Although thermostability in this enzyme class is generally low, there is not sufficient understanding of its basis for rational enzyme design. The gene expressing the Co-type NHase from the moderate thermophile, Geobacillus pallidus RAPc8 (NRRL B-59396), was subjected to random mutagenesis. Four mutants were selected that were 3 to 15-fold more thermostable than the wild-type NHase, resulting in a 3.4-7.6 ​kJ/mol increase in the activation energy of thermal inactivation at 63 ​ degrees C. High resolution X-ray crystal structures (1.15-1.80 ​A) were obtained of the wild-type and four mutant enzymes. Mutant 9E, with a resolution of 1.15 ​A, is the highest resolution crystal structure obtained for a nitrile hydratase to date. Structural comparisons between the wild-type and mutant enzymes illustrated the importance of salt bridges and hydrogen bonds in enhancing NHase thermostability. These additional interactions variously improved thermostability by increased intra- and inter-subunit interactions, preventing cooperative unfolding of alpha-helices and stabilising loop regions. Some hydrogen bonds were mediated via a water molecule, specifically highlighting the significance of structured water molecules in protein thermostability. Although knowledge of the mutant structures makes it possible to rationalize their behaviour, it would have been challenging to predict in advance that these mutants would be stabilising.


Authors: Van Wyk, J.C., Cowan, D.A., Danson, M.J., Tsekoa, T.L., Sayed, M.F., Sewell, B.T.
Engineering enhanced thermostability into the Geobacillus pallidus nitrile hydratase.,Van Wyk JC, Sewell BT, Danson MJ, Tsekoa TL, Sayed MF, Cowan DA Curr Res Struct Biol. 2022 Aug 19;4:256-270. doi: 10.1016/j.crstbi.2022.07.002. , eCollection 2022. PMID:36106339<ref>PMID:36106339</ref>


Description: A mutant of the nitrile hydratase from Geobacillus pallidus having enhanced thermostability
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Sayed, M.F]]
<div class="pdbe-citations 7qop" style="background-color:#fffaf0;"></div>
[[Category: Cowan, D.A]]
 
[[Category: Van Wyk, J.C]]
==See Also==
[[Category: Sewell, B.T]]
*[[Nitrile hydratase|Nitrile hydratase]]
[[Category: Tsekoa, T.L]]
== References ==
[[Category: Danson, M.J]]
<references/>
__TOC__
</StructureSection>
[[Category: Aeribacillus pallidus]]
[[Category: Large Structures]]
[[Category: Cowan DA]]
[[Category: Danson MJ]]
[[Category: Sayed MF]]
[[Category: Sewell BT]]
[[Category: Tsekoa TL]]
[[Category: Van Wyk JC]]

Latest revision as of 16:56, 6 November 2024

A mutant of the nitrile hydratase from Geobacillus pallidus having enhanced thermostabilityA mutant of the nitrile hydratase from Geobacillus pallidus having enhanced thermostability

Structural highlights

7qop is a 2 chain structure with sequence from Aeribacillus pallidus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q84FS5_9BACI

Publication Abstract from PubMed

Nitrile hydratases (NHases) are important biocatalysts for the enzymatic conversion of nitriles to industrially-important amides such as acrylamide and nicotinamide. Although thermostability in this enzyme class is generally low, there is not sufficient understanding of its basis for rational enzyme design. The gene expressing the Co-type NHase from the moderate thermophile, Geobacillus pallidus RAPc8 (NRRL B-59396), was subjected to random mutagenesis. Four mutants were selected that were 3 to 15-fold more thermostable than the wild-type NHase, resulting in a 3.4-7.6 ​kJ/mol increase in the activation energy of thermal inactivation at 63 ​ degrees C. High resolution X-ray crystal structures (1.15-1.80 ​A) were obtained of the wild-type and four mutant enzymes. Mutant 9E, with a resolution of 1.15 ​A, is the highest resolution crystal structure obtained for a nitrile hydratase to date. Structural comparisons between the wild-type and mutant enzymes illustrated the importance of salt bridges and hydrogen bonds in enhancing NHase thermostability. These additional interactions variously improved thermostability by increased intra- and inter-subunit interactions, preventing cooperative unfolding of alpha-helices and stabilising loop regions. Some hydrogen bonds were mediated via a water molecule, specifically highlighting the significance of structured water molecules in protein thermostability. Although knowledge of the mutant structures makes it possible to rationalize their behaviour, it would have been challenging to predict in advance that these mutants would be stabilising.

Engineering enhanced thermostability into the Geobacillus pallidus nitrile hydratase.,Van Wyk JC, Sewell BT, Danson MJ, Tsekoa TL, Sayed MF, Cowan DA Curr Res Struct Biol. 2022 Aug 19;4:256-270. doi: 10.1016/j.crstbi.2022.07.002. , eCollection 2022. PMID:36106339[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Van Wyk JC, Sewell BT, Danson MJ, Tsekoa TL, Sayed MF, Cowan DA. Engineering enhanced thermostability into the Geobacillus pallidus nitrile hydratase. Curr Res Struct Biol. 2022 Aug 19;4:256-270. PMID:36106339 doi:10.1016/j.crstbi.2022.07.002

7qop, resolution 1.80Å

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