4f6c: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(4 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 4f6c is ON HOLD  until Paper Publication
==Crystal structure of Aureusimine biosynthetic cluster reductase domain==
<StructureSection load='4f6c' size='340' side='right'caption='[[4f6c]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4f6c]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4F6C 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]] 2.812&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4f6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f6c OCA], [https://pdbe.org/4f6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f6c RCSB], [https://www.ebi.ac.uk/pdbsum/4f6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f6c ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H3JX00_STAAM A0A0H3JX00_STAAM]
<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.


Authors: Mok, M., Junop, M.
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>


Description: Crystal structure of Aureusimine biosynthetic cluster reductase domain
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4f6c" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus subsp. aureus Mu50]]
[[Category: Junop M]]
[[Category: Mok M]]

Latest revision as of 06:57, 27 November 2024

Crystal structure of Aureusimine biosynthetic cluster reductase domain

4f6c, resolution 2.81Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA