View source for 3wv4


==Crystal structure of VinN==
<StructureSection load='3wv4' size='340' side='right'caption='[[3wv4]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wv4]] 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</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>
== Function ==
[https://www.uniprot.org/uniprot/Q76KY2_STRHA Q76KY2_STRHA] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:25246523</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wv4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces halstedii]]
[[Category: Cieslak J]]
[[Category: Eguchi T]]
[[Category: Kudo F]]
[[Category: Miyanaga A]]
[[Category: Shinohara Y]]