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| | ==Crystal structure of VinN== | | ==Crystal structure of VinN== |
| - | <StructureSection load='3wv4' size='340' side='right' caption='[[3wv4]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='3wv4' size='340' side='right'caption='[[3wv4]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wv4]] is a 2 chain structure with sequence from [http://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=3WV4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WV4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wv4]] 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=3WV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WV4 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wv5|3wv5]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wv5|3wv5]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">vinN ([http://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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wv4 OCA], [http://pdbe.org/3wv4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wv4 RCSB], [http://www.ebi.ac.uk/pdbsum/3wv4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wv4 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=3wv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wv4 OCA], [https://pdbe.org/3wv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wv4 RCSB], [https://www.ebi.ac.uk/pdbsum/3wv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wv4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Actinomyces halstedii waksman and curtis 1916]] | | [[Category: Actinomyces halstedii waksman and curtis 1916]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Cieslak, J]] | | [[Category: Cieslak, J]] |
| | [[Category: Eguchi, T]] | | [[Category: Eguchi, T]] |
| Structural highlights
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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