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| | <StructureSection load='3n5f' size='340' side='right'caption='[[3n5f]], [[Resolution|resolution]] 2.75Å' scene=''> | | <StructureSection load='3n5f' size='340' side='right'caption='[[3n5f]], [[Resolution|resolution]] 2.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3n5f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N5F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3n5f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N5F FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</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]] 2.75Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">amaB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/N-carbamoyl-L-amino-acid_hydrolase N-carbamoyl-L-amino-acid hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.87 3.5.1.87] </span></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=3n5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n5f OCA], [https://pdbe.org/3n5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n5f RCSB], [https://www.ebi.ac.uk/pdbsum/3n5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n5f ProSAT]</span></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=3n5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n5f OCA], [https://pdbe.org/3n5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n5f RCSB], [https://www.ebi.ac.uk/pdbsum/3n5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n5f ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AMAB2_GEOSE AMAB2_GEOSE] |
| | <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 12980]] | + | [[Category: Geobacillus stearothermophilus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: N-carbamoyl-L-amino-acid hydrolase]]
| + | [[Category: Garcia-Pino A]] |
| - | [[Category: Garcia-Pino, A]] | + | [[Category: Gavira JA]] |
| - | [[Category: Gavira, J A]] | + | [[Category: Martinez-Rodriguez S]] |
| - | [[Category: Martinez-Rodriguez, S]] | + | |
| - | [[Category: Binding residue]]
| + | |
| - | [[Category: Carbamoylase]]
| + | |
| - | [[Category: Dimerization domain]]
| + | |
| - | [[Category: Evolution]]
| + | |
| - | [[Category: Hinge domain]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: M20 peptidase family]]
| + | |
| Structural highlights
Function
AMAB2_GEOSE
Publication Abstract from PubMed
N-Carbamoyl-l-amino acid amidohydrolases (l-carbamoylases) are important industrial enzymes used in kinetic resolution of racemic mixtures of N-carbamoyl-amino acids due to their strict enantiospecificity. In this work, we report the first l-carbamoylase structure belonging to Geobacillus stearothermophilus CECT43 (BsLcar), at a resolution of 2.7 A. Structural analysis of BsLcar and several members of the peptidase M20/M25/M40 family confirmed the expected conserved residues at the active site in this family, and site-directed mutagenesis revealed their relevance to substrate binding. We also found an unexpectedly conserved arginine residue (Arg(234) in BsLcar), proven to be critical for dimerization of the enzyme. The mutation of this sole residue resulted in a total loss of activity and prevented the formation of the dimer in BsLcar. Comparative studies revealed that the dimerization domain of the peptidase M20/M25/M40 family is a "small-molecule binding domain," allowing further evolutionary considerations for this enzyme family.
Mutational and structural analysis of L-N-carbamoylase reveals new insights into a peptidase m20/m25/m40 family member.,Martinez-Rodriguez S, Garcia-Pino A, Las Heras-Vazquez FJ, Clemente-Jimenez JM, Rodriguez-Vico F, Garcia-Ruiz JM, Loris R, Gavira JA J Bacteriol. 2012 Nov;194(21):5759-68. doi: 10.1128/JB.01056-12. Epub 2012 Aug, 17. PMID:22904279[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Martinez-Rodriguez S, Garcia-Pino A, Las Heras-Vazquez FJ, Clemente-Jimenez JM, Rodriguez-Vico F, Garcia-Ruiz JM, Loris R, Gavira JA. Mutational and structural analysis of L-N-carbamoylase reveals new insights into a peptidase m20/m25/m40 family member. J Bacteriol. 2012 Nov;194(21):5759-68. doi: 10.1128/JB.01056-12. Epub 2012 Aug, 17. PMID:22904279 doi:http://dx.doi.org/10.1128/JB.01056-12
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