View source for 4nte


==Crystal structure of DepH==
<StructureSection load='4nte' size='340' side='right'caption='[[4nte]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4nte]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chromobacterium_violaceum Chromobacterium violaceum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NTE 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4nte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nte OCA], [https://pdbe.org/4nte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nte RCSB], [https://www.ebi.ac.uk/pdbsum/4nte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nte ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A4ZPY8_CHRVL A4ZPY8_CHRVL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nature provides a rich source of compounds with diverse chemical structures and biological activities, among them, sulfur-containing metabolites from bacteria and fungi. Some of these compounds bear a disulfide moiety that is indispensable for their bioactivity. Specialized oxidoreductases such as GliT, HlmI, and DepH catalyze the formation of this disulfide bridge in the virulence factor gliotoxin, the antibiotic holomycin, and the anticancer drug romidepsin, respectively. We have examined all three enzymes by X-ray crystallography and activity assays. Despite their differently sized substrate binding clefts and hence, their diverse substrate preferences, a unifying reaction mechanism is proposed based on the obtained crystal structures and further supported by mutagenesis experiments.

Flavoenzyme-catalyzed formation of disulfide bonds in natural products.,Scharf DH, Groll M, Habel A, Heinekamp T, Hertweck C, Brakhage AA, Huber EM Angew Chem Int Ed Engl. 2014 Feb 17;53(8):2221-4. doi: 10.1002/anie.201309302., Epub 2014 Jan 20. PMID:24446392<ref>PMID:24446392</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4nte" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chromobacterium violaceum]]
[[Category: Large Structures]]
[[Category: Brakhage AA]]
[[Category: Groll M]]
[[Category: Habel A]]
[[Category: Heinekamp T]]
[[Category: Hertweck C]]
[[Category: Huber EM]]
[[Category: Scharf DH]]