4nte
From Proteopedia
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| - | ''' | + | ==Crystal structure of DepH== |
| + | <StructureSection load='4nte' size='340' side='right' caption='[[4nte]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4nte]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"chromobacterium_janthinum"_(zopf)_ford_1927 "chromobacterium janthinum" (zopf) ford 1927]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NTE FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ntc|4ntc]], [[4ntd|4ntd]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">depH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=536 "Chromobacterium janthinum" (Zopf) Ford 1927])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nte OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nte RCSB], [http://www.ebi.ac.uk/pdbsum/4nte PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Brakhage, A A.]] | ||
| + | [[Category: Groll, M.]] | ||
| + | [[Category: Habel, A.]] | ||
| + | [[Category: Heinekamp, T.]] | ||
| + | [[Category: Hertweck, C.]] | ||
| + | [[Category: Huber, E M.]] | ||
| + | [[Category: Scharf, D H.]] | ||
| + | [[Category: Disulfide bond]] | ||
| + | [[Category: Natural sulfur product]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Romidepsin]] | ||
Revision as of 12:29, 18 May 2014
Crystal structure of DepH
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