|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal Structure of Nitrile Hydratase from Pseudonocardia thermophila bound to Butaneboronic Acid via Crystal Soaking== | | ==Crystal Structure of Nitrile Hydratase from Pseudonocardia thermophila bound to Butaneboronic Acid via Crystal Soaking== |
| - | <StructureSection load='4ob2' size='340' side='right' caption='[[4ob2]], [[Resolution|resolution]] 1.52Å' scene=''> | + | <StructureSection load='4ob2' size='340' side='right'caption='[[4ob2]], [[Resolution|resolution]] 1.52Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ob2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OB2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ob2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudonocardia_thermophila Pseudonocardia thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OB2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BUB:1-BUTANE+BORONIC+ACID'>BUB</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene></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]] 1.52Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BUB:1-BUTANE+BORONIC+ACID'>BUB</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ob0|4ob0]], [[4ob1|4ob1]], [[4ob3|4ob3]]</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=4ob2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ob2 OCA], [https://pdbe.org/4ob2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ob2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ob2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ob2 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrile_hydratase Nitrile hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.84 4.2.1.84] </span></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=4ob2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ob2 OCA], [http://pdbe.org/4ob2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ob2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ob2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ob2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NHAA_PSETH NHAA_PSETH]] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. [[http://www.uniprot.org/uniprot/NHAB_PSETH NHAB_PSETH]] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. | + | [https://www.uniprot.org/uniprot/NHAA_PSETH NHAA_PSETH] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 28: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Nitrile hydratase]] | + | [[Category: Large Structures]] |
| - | [[Category: Dali, L]] | + | [[Category: Pseudonocardia thermophila]] |
| - | [[Category: Richard, H]] | + | [[Category: Dali L]] |
| - | [[Category: Rui, W]] | + | [[Category: Richard H]] |
| - | [[Category: Ruslan, S]] | + | [[Category: Rui W]] |
| - | [[Category: Salette, M]] | + | [[Category: Ruslan S]] |
| - | [[Category: Lyase]]
| + | [[Category: Salette M]] |
| - | [[Category: Nucleophile]]
| + | |
| Structural highlights
4ob2 is a 2 chain structure with sequence from Pseudonocardia thermophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.52Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
NHAA_PSETH NHase catalyzes the hydration of various nitrile compounds to the corresponding amides.
Publication Abstract from PubMed
Nitrile hydratase (NHase) catalyzes the hydration of nitriles to their corresponding commercially valuable amides at ambient temperatures and physiological pH. Several reaction mechanisms have been proposed for NHase enzymes; however, the source of the nucleophile remains a mystery. Boronic acids have been shown to be potent inhibitors of numerous hydrolytic enzymes due to the open shell of boron, which allows it to expand from a trigonal planar (sp(2)) form to a tetrahedral form (sp(3)). Therefore, we examined the inhibition of the Co-type NHase from Pseudonocardia thermophila JCM 3095 (PtNHase) by boronic acids via kinetics and X-ray crystallography. Both 1-butaneboronic acid (BuBA) and phenylboronic acid (PBA) function as potent competitive inhibitors of PtNHase. X-ray crystal structures for BuBA and PBA complexed to PtNHase were solved and refined at 1.5, 1.6, and 1.2 A resolution. The resulting PtNHase-boronic acid complexes represent a "snapshot" of reaction intermediates and implicate the cysteine-sulfenic acid ligand as the catalytic nucleophile, a heretofore unknown role for the alphaCys(113)-OH sulfenic acid ligand. Based on these data, a new mechanism of action for the hydration of nitriles by NHase is presented.
The active site sulfenic acid ligand in nitrile hydratases can function as a nucleophile.,Martinez S, Wu R, Sanishvili R, Liu D, Holz R J Am Chem Soc. 2014 Jan 29;136(4):1186-9. doi: 10.1021/ja410462j. Epub 2014 Jan, 13. PMID:24383915[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Martinez S, Wu R, Sanishvili R, Liu D, Holz R. The active site sulfenic acid ligand in nitrile hydratases can function as a nucleophile. J Am Chem Soc. 2014 Jan 29;136(4):1186-9. doi: 10.1021/ja410462j. Epub 2014 Jan, 13. PMID:24383915 doi:http://dx.doi.org/10.1021/ja410462j
|
