7xbv: Difference between revisions
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==Crystal structure of the adenylation domain of CmnG in complex with AMPCPP== | |||
<StructureSection load='7xbv' size='340' side='right'caption='[[7xbv]], [[Resolution|resolution]] 1.94Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7xbv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharothrix_mutabilis_subsp._capreolus Saccharothrix mutabilis subsp. capreolus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XBV 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]] 1.94Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=7xbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xbv OCA], [https://pdbe.org/7xbv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xbv RCSB], [https://www.ebi.ac.uk/pdbsum/7xbv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xbv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A6YEH8_STRMP A6YEH8_STRMP] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Capreomycidine (Cap) is a nonproteinogenic amino acid and building block of nonribosomal peptide (NRP) natural products. We report the formation and activation of Cap in capreomycin biosynthesis. CmnC and CmnD catalyzed hydroxylation and cyclization, respectively, of l-Arg to form l-Cap. l-Cap is then adenylated by CmnG-A before being incorporated into the nonribosomal peptide. The co-crystal structures of CmnG-A with l-Cap and adenosine nucleotides provide insights into the specificity and engineering opportunities of this unique adenylation domain. | |||
Characterization and Structural Determination of CmnG-A, the Adenylation Domain That Activates the Nonproteinogenic Amino Acid Capreomycidine in Capreomycin Biosynthesis.,Chen IH, Cheng T, Wang YL, Huang SJ, Hsiao YH, Lai YT, Toh SI, Chu J, Rudolf JD, Chang CY Chembiochem. 2022 Dec 16;23(24):e202200563. doi: 10.1002/cbic.202200563. Epub , 2022 Nov 16. PMID:36278314<ref>PMID:36278314</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Chang | <div class="pdbe-citations 7xbv" style="background-color:#fffaf0;"></div> | ||
[[Category: Chen | == References == | ||
[[Category: Wang | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharothrix mutabilis subsp. capreolus]] | |||
[[Category: Chang CY]] | |||
[[Category: Chen IH]] | |||
[[Category: Wang YL]] | |||
Latest revision as of 17:51, 29 November 2023
Crystal structure of the adenylation domain of CmnG in complex with AMPCPP
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