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| | <StructureSection load='5g3p' size='340' side='right'caption='[[5g3p]], [[Resolution|resolution]] 1.78Å' scene=''> | | <StructureSection load='5g3p' size='340' side='right'caption='[[5g3p]], [[Resolution|resolution]] 1.78Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5g3p]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G3P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5G3P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5g3p]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G3P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.78Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5g3o|5g3o]]</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=5g3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g3p OCA], [https://pdbe.org/5g3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g3p RCSB], [https://www.ebi.ac.uk/pdbsum/5g3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g3p ProSAT]</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=5g3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g3p OCA], [http://pdbe.org/5g3p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g3p RCSB], [http://www.ebi.ac.uk/pdbsum/5g3p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g3p ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/E5LR94_BACCE E5LR94_BACCE]] Is an aliphatic amidase with a restricted substrate specificity, as it only hydrolyzes formamide.[HAMAP-Rule:MF_01243] | + | [https://www.uniprot.org/uniprot/AMIF_BACCR AMIF_BACCR] Is an aliphatic amidase with a restricted substrate specificity, as it only hydrolyzes formamide.[HAMAP-Rule:MF_01243] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 14579]] | + | [[Category: Bacillus cereus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Conejero-Muriel, M]] | + | [[Category: Conejero-Muriel M]] |
| - | [[Category: Gavira, J A]] | + | [[Category: Gavira JA]] |
| - | [[Category: Martinez-Rodriguez, S]] | + | [[Category: Martinez-Rodriguez S]] |
| - | [[Category: Amidase]]
| + | |
| - | [[Category: Formamidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nitrilase superfamily]]
| + | |
| Structural highlights
5g3p is a 6 chain structure with sequence from Bacillus cereus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.78Å |
| Ligands: | , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
AMIF_BACCR Is an aliphatic amidase with a restricted substrate specificity, as it only hydrolyzes formamide.[HAMAP-Rule:MF_01243]
Publication Abstract from PubMed
Formamidases (EC 3.5.1.49) and amidases (EC 3.5.1.4) are paralogous cysteine-dependent enzymes which catalyze the conversion of amide substrates to ammonia and the corresponding carboxylic acid. Both enzymes have been suggested as an alternative pathway for ammonia production during urea shortage. Urea was proved key in the transcriptional regulation of formamidases/amidases, connecting urea level to amide metabolism. In addition, different amidases have also been shown to be inhibited by urea, pointing to urea-regulation at the enzymatic level. Although amidases have been widely studied due to its biotechnological application in the hydrolysis of aliphatic amides, up to date, only two formamidases have been extensively characterized, belonging to Helicobacter pylori (HpyAmiF) and Bacillus cereus (BceAmiF). In this work, we report the first structure of an acyl-intermediate of BceAmiF. We also report the inhibition of BceAmiF by urea, together with mass spectrometry studies confirming the S-carbamoylation of BceAmiF after urea treatment. X-ray studies of urea-soaked BceAmiF crystals showed short- and long-range rearrangements affecting oligomerization interfaces. Since cysteine-based switches are known to occur in the regulation of different metabolic and signaling pathways, our results suggest a novel S-carbamoylation-switch for the regulation of BceAmiF. This finding could relate to previous observations of unexplained modifications in the catalytic cysteine of different nitrilase superfamily members and therefore extending this regulation mechanism to the whole nitrilase superfamily.
A novel cysteine carbamoyl-switch is responsible for the inhibition of formamidase, a nitrilase superfamily member.,Martinez-Rodriguez S, Conejero-Muriel M, Gavira JA Arch Biochem Biophys. 2019 Feb 15;662:151-159. doi: 10.1016/j.abb.2018.12.008., Epub 2018 Dec 5. PMID:30528776[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Martinez-Rodriguez S, Conejero-Muriel M, Gavira JA. A novel cysteine carbamoyl-switch is responsible for the inhibition of formamidase, a nitrilase superfamily member. Arch Biochem Biophys. 2019 Feb 15;662:151-159. doi: 10.1016/j.abb.2018.12.008., Epub 2018 Dec 5. PMID:30528776 doi:http://dx.doi.org/10.1016/j.abb.2018.12.008
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