3u4c: Difference between revisions
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<StructureSection load='3u4c' size='340' side='right' caption='[[3u4c]], [[Resolution|resolution]] 2.03Å' scene=''> | <StructureSection load='3u4c' size='340' side='right' caption='[[3u4c]], [[Resolution|resolution]] 2.03Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3u4c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/" | <table><tr><td colspan='2'>[[3u4c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U4C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U4C FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3u49|3u49]], [[3u4d|3u4d]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3u49|3u49]], [[3u4d|3u4d]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU37680, ipa-86r, ywfH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 " | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU37680, ipa-86r, ywfH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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=3u4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u4c OCA], [http://pdbe.org/3u4c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u4c RCSB], [http://www.ebi.ac.uk/pdbsum/3u4c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u4c ProSAT]</span></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=3u4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u4c OCA], [http://pdbe.org/3u4c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u4c RCSB], [http://www.ebi.ac.uk/pdbsum/3u4c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u4c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Vibrio subtilis ehrenberg 1835]] | ||
[[Category: Gopal, B]] | [[Category: Gopal, B]] | ||
[[Category: Rajavel, M]] | [[Category: Rajavel, M]] | ||
Revision as of 17:39, 15 November 2017
Crystal structure of YwfH, NADPH dependent reductase involved in Bacilysin biosynthesisCrystal structure of YwfH, NADPH dependent reductase involved in Bacilysin biosynthesis
Structural highlights
Function[YWFH_BACSU] Along with the bacABCDE operon is involved in bacilysin biosynthesis. Publication Abstract from PubMedThe synthesis of the dipeptide antibiotic bacilysin involves the sequential action of multiple enzymes in the bac operon. YwfH (also referred to as BacG) catalyzes the stereoselective reduction of dihydro-hydroxyphenylpyruvate (H2HPP) to tetrahydro-hydroxyphenylpyruvate (H4HPP) in this biosynthetic pathway. YwfH is an NADPH-dependent reductase that facilitates the conjugate addition of a hydride at the C4 olefin terminus of H2HPP. Here, the structure of YwfH is described at three conformational steps: the apo form, an apo-like conformation and the NADPH complex. YwfH is structurally similar to other characterized short-chain dehydrogenase/reductases despite having marginal sequence similarity. The structures of YwfH in different conformational states provide a rationale for the ping-pong reaction mechanism. The identification and role of the residues in the catalytic tetrad (Lys113-Tyr117-Ser155-Asn158) in proton transfer were examined by mutational analysis. Together, the structures and biochemical features revealed synchronized conformational changes that facilitate cofactor specificity and catalysis of H4HPP formation en route to tetrahydrotyrosine synthesis. Structural insights into the role of Bacillus subtilis YwfH (BacG) in tetrahydrotyrosine synthesis.,Rajavel M, Perinbam K, Gopal B Acta Crystallogr D Biol Crystallogr. 2013 Mar;69(Pt 3):324-32. doi:, 10.1107/S0907444912046690. Epub 2013 Feb 16. PMID:23519407[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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