5wmm: Difference between revisions

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'''Unreleased structure'''


The entry 5wmm is ON HOLD  until Paper Publication
==Crystal structure of an adenylation domain interrupted by a methylation domain (AMA4) from nonribosomal peptide synthetase TioS==
<StructureSection load='5wmm' size='340' side='right'caption='[[5wmm]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5wmm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonospora_sp._ML1 Micromonospora sp. ML1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WMM 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]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B6G:(2S)-2-amino-3-methylbutanoyl+(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl+hydrogen+(S)-phosphate'>B6G</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=5wmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wmm OCA], [https://pdbe.org/5wmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wmm RCSB], [https://www.ebi.ac.uk/pdbsum/5wmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wmm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q333U7_9ACTN Q333U7_9ACTN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Interrupted adenylation domains are enigmatic fusions, in which one enzyme is inserted into another to form a highly unusual bifunctional enzyme. We present the first crystal structure of an interrupted adenylation domain that reveals a unique embedded methyltransferase. The structure and functional data provide insight into how these enzymes N-methylate amino acid precursors en route to nonribosomal peptides.


Authors:  
Structural basis for backbone N-methylation by an interrupted adenylation domain.,Mori S, Pang AH, Lundy TA, Garzan A, Tsodikov OV, Garneau-Tsodikova S Nat Chem Biol. 2018 Mar 19. pii: 10.1038/s41589-018-0014-7. doi:, 10.1038/s41589-018-0014-7. PMID:29556104<ref>PMID:29556104</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5wmm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Micromonospora sp. ML1]]
[[Category: Garneau-Tsodikova S]]
[[Category: Mori S]]
[[Category: Pang AH]]
[[Category: Tsodikov OV]]
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