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| | ==Crystal structure of Co-type nitrile hydratase complexed with n-butyric acid== | | ==Crystal structure of Co-type nitrile hydratase complexed with n-butyric acid== |
| - | <StructureSection load='1ugp' size='340' side='right' caption='[[1ugp]], [[Resolution|resolution]] 1.63Å' scene=''> | + | <StructureSection load='1ugp' size='340' side='right'caption='[[1ugp]], [[Resolution|resolution]] 1.63Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ugp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_19285 Atcc 19285]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UGP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UGP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ugp]] 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=1UGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UGP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BUA:BUTANOIC+ACID'>BUA</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BUA:BUTANOIC+ACID'>BUA</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></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>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</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=1ugp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ugp OCA], [https://pdbe.org/1ugp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ugp RCSB], [https://www.ebi.ac.uk/pdbsum/1ugp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ugp ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ire|1ire]], [[1ugq|1ugq]], [[1ugr|1ugr]], [[1ugs|1ugs]]</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=1ugp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ugp OCA], [http://pdbe.org/1ugp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ugp RCSB], [http://www.ebi.ac.uk/pdbsum/1ugp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ugp 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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 19285]] | + | [[Category: Large Structures]] |
| - | [[Category: Nitrile hydratase]] | + | [[Category: Pseudonocardia thermophila]] |
| - | [[Category: Fushinobu, S]] | + | [[Category: Fushinobu S]] |
| - | [[Category: Ito, K]] | + | [[Category: Ito K]] |
| - | [[Category: Miyanaga, A]] | + | [[Category: Miyanaga A]] |
| - | [[Category: Shoun, H]] | + | [[Category: Shoun H]] |
| - | [[Category: Wakagi, T]] | + | [[Category: Wakagi T]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Hydration]]
| + | |
| - | [[Category: Lyase]]
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| - | [[Category: N-butyric acid]]
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| - | [[Category: Nitrile]]
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| - | [[Category: Non-corrin cobalt]]
| + | |
| Structural highlights
Function
NHAA_PSETH NHase catalyzes the hydration of various nitrile compounds to the corresponding amides.
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 PubMed
Mutants of a cobalt-containing nitrile hydratase (NHase, EC 4.2.1.84) from Pseudonocardia thermophila JCM 3095 involved in substrate binding, catalysis and formation of the active center were constructed, and their characteristics and crystal structures were investigated. As expected from the structure of the substrate binding pocket, the wild-type enzyme showed significantly lower K(m) and K(i) values for aromatic substrates and inhibitors, respectively, than aliphatic ones. In the crystal structure of a complex with an inhibitor (n-butyric acid) the hydroxyl group of betaTyr68 formed hydrogen bonds with both n-butyric acid and alphaSer112, which is located in the active center. The betaY68F mutant showed an elevated K(m) value and a significantly decreased k(cat) value. The apoenzyme, which contains no detectable cobalt atom, was prepared from Escherichia coli cells grown in medium without cobalt ions. It showed no detectable activity. A disulfide bond between alphaCys108 and alphaCys113 was formed in the apoenzyme structure. In the highly conserved sequence motif in the cysteine cluster region, two positions are exclusively conserved in cobalt-containing or iron-containing nitrile hydratases. Two mutants (alphaT109S and alphaY114T) were constructed, each residue being replaced with an iron-containing one. The alphaT109S mutant showed similar characteristics to the wild-type enzyme. However, the alphaY114T mutant showed a very low cobalt content and catalytic activity compared with the wild-type enzyme, and oxidative modifications of alphaCys111 and alphaCys113 residues were not observed. The alphaTyr114 residue may be involved in the interaction with the nitrile hydratase activator protein of P. thermophila.
Mutational and structural analysis of cobalt-containing nitrile hydratase on substrate and metal binding.,Miyanaga A, Fushinobu S, Ito K, Shoun H, Wakagi T Eur J Biochem. 2004 Jan;271(2):429-38. PMID:14717710[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Miyanaga A, Fushinobu S, Ito K, Shoun H, Wakagi T. Mutational and structural analysis of cobalt-containing nitrile hydratase on substrate and metal binding. Eur J Biochem. 2004 Jan;271(2):429-38. PMID:14717710
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