4f6c: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[ | ==Crystal structure of Aureusimine biosynthetic cluster reductase domain== | ||
<StructureSection load='4f6c' size='340' side='right' caption='[[4f6c]], [[Resolution|resolution]] 2.81Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4f6c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_mu50 Staphylococcus aureus subsp. aureus mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F6C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F6C FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f6l|4f6l]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAV0179 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158878 Staphylococcus aureus subsp. aureus Mu50])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f6c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f6c RCSB], [http://www.ebi.ac.uk/pdbsum/4f6c PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Through a number of strategies nonribosomal peptide assembly lines give rise to a metabolic diversity not possible by ribosomal synthesis. One distinction within nonribosomal assembly is that products are elaborated on an enzyme-tethered substrate, and their release is enzyme catalysed. Reductive release by NAD(P)H-dependent catalysts is one observed nonribosomal termination and release strategy. Here we probed the selectivity of a terminal reductase domain by using a full-length heterologously expressed nonribosomal peptide synthetase for the dipeptide aureusimine and were able to generate 17 new analogues. Further, we generated an X-ray structure of aureusimine terminal reductase to gain insight into the structural details associated with this enzymatic domain. | |||
Heterologous expression and structural characterisation of a pyrazinone natural product assembly line.,Wyatt MA, Mok MC, Junop M, Magarvey NA Chembiochem. 2012 Nov 5;13(16):2408-15. doi: 10.1002/cbic.201200340. Epub 2012, Oct 15. PMID:23070851<ref>PMID:23070851</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Staphylococcus aureus subsp. aureus mu50]] | [[Category: Staphylococcus aureus subsp. aureus mu50]] | ||
[[Category: Junop, M | [[Category: Junop, M]] | ||
[[Category: Mok, M | [[Category: Mok, M]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Thioester reductase]] | [[Category: Thioester reductase]] | ||
Revision as of 14:00, 4 January 2015
Crystal structure of Aureusimine biosynthetic cluster reductase domain
| ||||||||||||