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| | <StructureSection load='3uao' size='340' side='right'caption='[[3uao]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='3uao' size='340' side='right'caption='[[3uao]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3uao]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/"alcaligenes_bronchicanis"_(ferry_1911)_haupt_1935 "alcaligenes bronchicanis" (ferry 1911) haupt 1935]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UAO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UAO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3uao]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_bronchiseptica Bordetella bronchiseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UAO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UAO FirstGlance]. <br> |
| - | </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></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]] 2.399Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</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=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ilw|1ilw]], [[1nba|1nba]], [[1yac|1yac]], [[1im5|1im5]], [[3gbc|3gbc]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BB0275, BB1782 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=518 "Alcaligenes bronchicanis" (Ferry 1911) Haupt 1935])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Maleamate_amidohydrolase Maleamate amidohydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.107 3.5.1.107] </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=3uao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uao OCA], [https://pdbe.org/3uao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uao RCSB], [https://www.ebi.ac.uk/pdbsum/3uao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uao 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=3uao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uao OCA], [https://pdbe.org/3uao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uao RCSB], [https://www.ebi.ac.uk/pdbsum/3uao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uao ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0H3LKK8_BORBR A0A0H3LKK8_BORBR] |
| | <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: Bordetella bronchiseptica]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Maleamate amidohydrolase]]
| + | [[Category: Kincaid VA]] |
| - | [[Category: Kincaid, V A]] | + | [[Category: Klein RD]] |
| - | [[Category: Klein, R D]] | + | [[Category: Rowlett RS]] |
| - | [[Category: Rowlett, R S]] | + | [[Category: Snider MJ]] |
| - | [[Category: Snider, M J]] | + | [[Category: Sullivan ED]] |
| - | [[Category: Sullivan, E D]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Maleamate]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
A0A0H3LKK8_BORBR
Publication Abstract from PubMed
The penultimate reaction in the oxidative degradation of nicotinate (vitamin B(3)) to fumarate in several species of aerobic bacteria is the hydrolytic deamination of maleamate to maleate, catalyzed by maleamate amidohydrolase (NicF). Although it has been considered a model system for bacterial degradation of N-heterocyclic compounds, only recently have gene clusters that encode the enzymes of this catabolic pathway been identified to allow detailed investigations concerning the structural basis of their mechanisms. Here, the Bb1774 gene from Bordetella bronchiseptica RB50, putatively annotated as nicF, has been cloned, and the recombinant enzyme, overexpressed and purified from Escherichia coli, is shown to catalyze efficiently the hydrolysis of maleamate to maleate and ammonium ion. Steady-state kinetic analysis of the reaction by isothermal titration calorimetry (ITC) established k(cat) and K(M) values (pH 7.5 and 25 degrees C) of 11.7 +/- 0.2 s(-1) and 128 +/- 6 muM, respectively. The observed K(D) of the NicF.maleate (E.P) complex, also measured by ITC, is approximated to be 3.8 +/- 0.4 mM. The crystal structure of NicF, determined at 2.4 A using molecular replacement, shows that the enzyme belongs to the cysteine hydrolase superfamily. The structure provides insight concerning the roles of potential catalytically important residues, most notably a conserved catalytic triad (Asp29, Lys117, and Cys150) observed in the proximity of a conserved non-proline cis-peptide bond within a small cavity that is likely the active site. On the basis of this structural information, the hydrolysis of maleamate is proposed to proceed by a nucleophilic addition-elimination sequence involving the thiolate side chain of Cys150.
Structure and Catalytic Mechanism of Nicotinate (Vitamin B(3)) Degradative Enzyme Maleamate Amidohydrolase from Bordetella bronchiseptica RB50.,Kincaid VA, Sullivan ED, Klein RD, Noel JW, Rowlett RS, Snider MJ Biochemistry. 2012 Jan 10;51(1):545-54. Epub 2011 Dec 23. PMID:22214383[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kincaid VA, Sullivan ED, Klein RD, Noel JW, Rowlett RS, Snider MJ. Structure and Catalytic Mechanism of Nicotinate (Vitamin B(3)) Degradative Enzyme Maleamate Amidohydrolase from Bordetella bronchiseptica RB50. Biochemistry. 2012 Jan 10;51(1):545-54. Epub 2011 Dec 23. PMID:22214383 doi:10.1021/bi201347n
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