4ntc
From Proteopedia
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| - | ''' | + | ==Crystal structure of GliT== |
| + | <StructureSection load='4ntc' size='340' side='right' caption='[[4ntc]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ntc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfm Aspfm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NTC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NTC FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fbs|3fbs]], [[4ntd|4ntd]], [[4nte|4nte]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gliT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=746128 ASPFM])</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=4ntc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ntc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ntc RCSB], [http://www.ebi.ac.uk/pdbsum/4ntc 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: Aspfm]] | ||
| + | [[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: Epipolythiodioxopiperazine]] | ||
| + | [[Category: Gliotoxin]] | ||
| + | [[Category: Natural sulfur product]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 12:28, 18 May 2014
Crystal structure of GliT
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