View source for 5jjp


==Crystal structure of CmiS6==
<StructureSection load='5jjp' size='340' side='right'caption='[[5jjp]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jjp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._MJ635-86F5 Streptomyces sp. MJ635-86F5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JJP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JJP 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]] 2.3&#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=5jjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jjp OCA], [https://pdbe.org/5jjp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jjp RCSB], [https://www.ebi.ac.uk/pdbsum/5jjp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jjp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/X5IJ97_9ACTN X5IJ97_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Macrolactam antibiotics such as incednine and cremimycin possess an aliphatic beta-amino acid as a starter unit of their polyketide chain. In the biosynthesis of incednine and cremimycin, unique stand-alone adenylation enzymes IdnL1 and CmiS6 select and activate the proper aliphatic beta-amino acid as a starter unit. In this study, we describe the enzymatic characterization and the structural basis of substrate specificity of IdnL1 and CmiS6. Functional analysis revealed that IdnL1 and CmiS6 recognize 3-aminobutanoic acid and 3-aminononanoic acid, respectively. We solved the X-ray crystal structures of IdnL1 and CmiS6 to understand the recognition mechanism of these aliphatic beta-amino acids. These structures revealed that IdnL1 and CmiS6 share a common recognition motif that interacts with the beta-amino group of the substrates. However, the hydrophobic side-chains of the substrates are accommodated differently in the two enzymes. IdnL1 has a bulky Leu220 located close to the terminal methyl group of 3-aminobutanoate of the trapped acyl-adenylate intermediate to construct a shallow substrate-binding pocket. In contrast, CmiS6 possesses Gly220 at the corresponding position to accommodate 3-aminononanoic acid. This structural observation was supported by a mutational study. Thus, the size of amino acid residue at the 220 position is critical for the selection of an aliphatic beta-amino acid substrate in these adenylation enzymes. Proteins 2017; 85:1238-1247. (c) 2017 Wiley Periodicals, Inc.

Biochemical characterization and structural insight into aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6.,Cieslak J, Miyanaga A, Takaku R, Takaishi M, Amagai K, Kudo F, Eguchi T Proteins. 2017 Jul;85(7):1238-1247. doi: 10.1002/prot.25284. Epub 2017 Mar 29. PMID:28316096<ref>PMID:28316096</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5jjp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp. MJ635-86F5]]
[[Category: Cieslak J]]
[[Category: Eguchi T]]
[[Category: Kudo F]]
[[Category: Miyanaga A]]