1zz7: Difference between revisions
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==Crystal Structure of FeII HppE in Complex with Substrate form 1== | ==Crystal Structure of FeII HppE in Complex with Substrate form 1== | ||
<StructureSection load='1zz7' size='340' side='right' caption='[[1zz7]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1zz7' size='340' side='right' caption='[[1zz7]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zz6|1zz6]], [[1zz8|1zz8]], [[1zz9|1zz9]], [[1zzb|1zzb]], [[1zzc|1zzc]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zz6|1zz6]], [[1zz8|1zz8]], [[1zz9|1zz9]], [[1zzb|1zzb]], [[1zzc|1zzc]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fom4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43759 "Actinomyces wedmorensis" Milard and Burr 1926])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fom4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43759 "Actinomyces wedmorensis" Milard and Burr 1926])</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=1zz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zz7 OCA], [http://pdbe.org/1zz7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zz7 RCSB], [http://www.ebi.ac.uk/pdbsum/1zz7 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=1zz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zz7 OCA], [http://pdbe.org/1zz7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zz7 RCSB], [http://www.ebi.ac.uk/pdbsum/1zz7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zz7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zz/1zz7_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zz/1zz7_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 12:07, 2 May 2018
Crystal Structure of FeII HppE in Complex with Substrate form 1Crystal Structure of FeII HppE in Complex with Substrate form 1
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 biosynthetic pathway of the clinically important antibiotic fosfomycin uses enzymes that catalyse reactions without precedent in biology. Among these is hydroxypropylphosphonic acid epoxidase, which represents a new subfamily of non-haem mononuclear iron enzymes. Here we present six X-ray structures of this enzyme: the apoenzyme at 2.0 A resolution; a native Fe(II)-bound form at 2.4 A resolution; a tris(hydroxymethyl)aminomethane-Co(II)-enzyme complex structure at 1.8 A resolution; a substrate-Co(II)-enzyme complex structure at 2.5 A resolution; and two substrate-Fe(II)-enzyme complexes at 2.1 and 2.3 A resolution. These structural data lead us to suggest how this enzyme is able to recognize and respond to its substrate with a conformational change that protects the radical-based intermediates formed during catalysis. Comparisons with other family members suggest why substrate binding is able to prime iron for dioxygen binding in the absence of alpha-ketoglutarate (a co-substrate required by many mononuclear iron enzymes), and how the unique epoxidation reaction of hydroxypropylphosphonic acid epoxidase may occur. Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme.,Higgins LJ, Yan F, Liu P, Liu HW, Drennan CL Nature. 2005 Oct 6;437(7060):838-44. Epub 2005 Jul 13. PMID:16015285[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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