6akd
From Proteopedia
(Difference between revisions)
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of IdnL7== | |
| + | <StructureSection load='6akd' size='340' side='right'caption='[[6akd]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6akd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._ML694-90F3 Streptomyces sp. ML694-90F3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AKD 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]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A5A:5-O-(N-(L-ALANYL)-SULFAMOYL)ADENOSINE'>A5A</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=6akd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6akd OCA], [https://pdbe.org/6akd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6akd RCSB], [https://www.ebi.ac.uk/pdbsum/6akd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6akd ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A077KUW8_9ACTN A0A077KUW8_9ACTN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Adenylation enzymes play an important role in the selective incorporation of the cognate carboxylate substrates in natural product biosynthesis. Here, the biochemical and structural characterization of the adenylation enzyme IdnL7, which is involved in the biosynthesis of the macrolactam polyketide antibiotic incednine, is reported. Biochemical analysis showed that IdnL7 selects and activates several small amino acids. The structure of IdnL7 in complex with an L-alanyl-adenylate intermediate mimic, 5'-O-[N-(L-alanyl)sulfamoyl]adenosine, was determined at 2.1 A resolution. The structure of IdnL7 explains the broad substrate specificity of IdnL7 towards small L-amino acids. | ||
| - | + | Functional and structural characterization of IdnL7, an adenylation enzyme involved in incednine biosynthesis.,Cieslak J, Miyanaga A, Takaishi M, Kudo F, Eguchi T Acta Crystallogr F Struct Biol Commun. 2019 Apr 1;75(Pt 4):299-306. doi:, 10.1107/S2053230X19002863. Epub 2019 Apr 2. PMID:30950831<ref>PMID:30950831</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6akd" style="background-color:#fffaf0;"></div> |
| - | [[Category: Cieslak | + | == References == |
| - | [[Category: Kudo | + | <references/> |
| - | [[Category: Miyanaga | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces sp. ML694-90F3]] | ||
| + | [[Category: Cieslak J]] | ||
| + | [[Category: Eguchi T]] | ||
| + | [[Category: Kudo F]] | ||
| + | [[Category: Miyanaga A]] | ||
Current revision
Crystal structure of IdnL7
| |||||||||||
