2bno: Difference between revisions
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<StructureSection load='2bno' size='340' side='right' caption='[[2bno]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2bno' size='340' side='right' caption='[[2bno]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2bno]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2bno]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_wedmorensis"_milard_and_burr_1926 "actinomyces wedmorensis" milard and burr 1926]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BNO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BNO FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zz9|1zz9]], [[2bnm|2bnm]], [[1zz7|1zz7]], [[1zz6|1zz6]], [[1zz8|1zz8]], [[1zzb|1zzb]], [[1zzc|1zzc]], [[2bnn|2bnn]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zz9|1zz9]], [[2bnm|2bnm]], [[1zz7|1zz7]], [[1zz6|1zz6]], [[1zz8|1zz8]], [[1zzb|1zzb]], [[1zzc|1zzc]], [[2bnn|2bnn]]</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=2bno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bno OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bno RCSB], [http://www.ebi.ac.uk/pdbsum/2bno PDBsum]</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=2bno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bno OCA], [http://pdbe.org/2bno PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bno RCSB], [http://www.ebi.ac.uk/pdbsum/2bno PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2bno" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Actinomyces wedmorensis milard and burr 1926]] | ||
[[Category: Cameron, S]] | [[Category: Cameron, S]] | ||
[[Category: Hunter, W N]] | [[Category: Hunter, W N]] | ||
Revision as of 10:11, 10 September 2015
THE STRUCTURE OF HYDROXYPROPYLPHOSPHONIC ACID EPOXIDASE FROM S. WEDMORENIS.THE STRUCTURE OF HYDROXYPROPYLPHOSPHONIC ACID EPOXIDASE FROM S. WEDMORENIS.
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe biosynthesis of fosfomycin, an oxirane antibiotic in clinical use, involves a unique epoxidation catalyzed by (S)-2-hydroxypropylphosphonic acid epoxidase (HPPE). The reaction is essentially dehydrogenation of a secondary alcohol. A high-resolution crystallographic analysis reveals that the HPPE subunit displays a two-domain combination. The C-terminal or catalytic domain has the cupin fold that binds a divalent cation, whereas the N-terminal domain carries a helix-turn-helix motif with putative DNA-binding helices positioned 34 A apart. The structure of HPPE serves as a model for numerous proteins, of ill-defined function, predicted to be transcription factors but carrying a cupin domain at the C terminus. Structure-reactivity analyses reveal conformational changes near the catalytic center driven by the presence or absence of ligand, that HPPE is a Zn(2+)/Fe(2+)-dependent epoxidase, proof that flavin mononucleotide is required for catalysis, and allow us to propose a simple mechanism that is compatible with previous experimental data. The participation of the redox inert Zn(2+) in the mechanism is surprising and indicates that Lewis acid properties of the metal ions are sufficient to polarize the substrate and, aided by flavin mononucleotide reduction, facilitate the epoxidation. Structure and reactivity of hydroxypropylphosphonic acid epoxidase in fosfomycin biosynthesis by a cation- and flavin-dependent mechanism.,McLuskey K, Cameron S, Hammerschmidt F, Hunter WN Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14221-6. Epub 2005 Sep 26. PMID:16186494[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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