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| | <StructureSection load='3wv5' size='340' side='right'caption='[[3wv5]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='3wv5' size='340' side='right'caption='[[3wv5]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wv5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinomyces_halstedii"_waksman_and_curtis_1916 "actinomyces halstedii" waksman and curtis 1916]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WV5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WV5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wv5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_halstedii Streptomyces halstedii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WV5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WV5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2AS:(2S,3S)-3-METHYL-ASPARTIC+ACID'>2AS</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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wv4|3wv4]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2AS:(2S,3S)-3-METHYL-ASPARTIC+ACID'>2AS</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">vinN ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1944 "Actinomyces halstedii" Waksman and Curtis 1916])</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=3wv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wv5 OCA], [https://pdbe.org/3wv5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wv5 RCSB], [https://www.ebi.ac.uk/pdbsum/3wv5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wv5 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=3wv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wv5 OCA], [https://pdbe.org/3wv5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wv5 RCSB], [https://www.ebi.ac.uk/pdbsum/3wv5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wv5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q76KY2_STRHA Q76KY2_STRHA] |
| | <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: Actinomyces halstedii waksman and curtis 1916]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cieslak, J]] | + | [[Category: Streptomyces halstedii]] |
| - | [[Category: Eguchi, T]] | + | [[Category: Cieslak J]] |
| - | [[Category: Kudo, F]] | + | [[Category: Eguchi T]] |
| - | [[Category: Miyanaga, A]] | + | [[Category: Kudo F]] |
| - | [[Category: Shinohara, Y]] | + | [[Category: Miyanaga A]] |
| - | [[Category: Atp binding]]
| + | [[Category: Shinohara Y]] |
| - | [[Category: Five-layered alpha-beta-alpha-beta-alpha sandwich fold]]
| + | |
| - | [[Category: Ligase]]
| + | |
| Structural highlights
Function
Q76KY2_STRHA
Publication Abstract from PubMed
Adenylation enzymes play important roles in the biosynthesis and degradation of primary and secondary metabolites. Mechanistic insights into the recognition of alpha-amino acid substrates have been obtained for alpha-amino acid adenylation enzymes. The Asp residue is invariant and is essential for the stabilization of the alpha-amino group of the substrate. In contrast, the beta-amino acid recognition mechanism of adenylation enzymes is still unclear despite the importance of beta-amino acid activation for the biosynthesis of various natural products. Herein, we report the crystal structure of the stand-alone adenylation enzyme VinN, which specifically activates (2S,3S)-3-methylaspartate (3-MeAsp) in vicenistatin biosynthesis. VinN has an overall structure similar to that of other adenylation enzymes. The structure of the complex with 3-MeAsp revealed that a conserved Asp(230) residue is used in the recognition of the beta-amino group of 3-MeAsp similar to alpha-amino acid adenylation enzymes. A mutational analysis and structural comparison with alpha-amino acid adenylation enzymes showed that the substrate-binding pocket of VinN has a unique architecture to accommodate 3-MeAsp as a beta-amino acid substrate. Thus, the VinN structure allows the first visualization of the interaction of an adenylation enzyme with a beta-amino acid and provides new mechanistic insights into the selective recognition of beta-amino acids in this family of enzymes.
The crystal structure of the adenylation enzyme VinN reveals a unique beta-amino acid recognition mechanism.,Miyanaga A, Cieslak J, Shinohara Y, Kudo F, Eguchi T J Biol Chem. 2014 Nov 7;289(45):31448-57. doi: 10.1074/jbc.M114.602326. Epub 2014, Sep 22. PMID:25246523[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Miyanaga A, Cieslak J, Shinohara Y, Kudo F, Eguchi T. The crystal structure of the adenylation enzyme VinN reveals a unique beta-amino acid recognition mechanism. J Biol Chem. 2014 Nov 7;289(45):31448-57. doi: 10.1074/jbc.M114.602326. Epub 2014, Sep 22. PMID:25246523 doi:http://dx.doi.org/10.1074/jbc.M114.602326
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