1zz7

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[[Image:1zz7.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of FeII HppE in Complex with Substrate form 1==
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|PDB= 1zz7 |SIZE=350|CAPTION= <scene name='initialview01'>1zz7</scene>, resolution 2.10&Aring;
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<StructureSection load='1zz7' size='340' side='right'caption='[[1zz7]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=S0H:(S)-2-HYDROXYPROPYLPHOSPHONIC+ACID'>S0H</scene>
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<table><tr><td colspan='2'>[[1zz7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_wedmorensis Streptomyces wedmorensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZZ7 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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|GENE= fom4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43759 Streptomyces wedmorensis])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=S0H:(S)-2-HYDROXYPROPYLPHOSPHONIC+ACID'>S0H</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zz7 OCA], [https://pdbe.org/1zz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zz7 RCSB], [https://www.ebi.ac.uk/pdbsum/1zz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zz7 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1zz6|1ZZ6]], [[1zz8|1ZZ8]], [[1zz9|1ZZ9]], [[1zzb|1ZZB]], [[1zzc|1ZZC]]
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</table>
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1zz7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zz7 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/HPPE_STRWE HPPE_STRWE] Non-heme-dependent dioxygenase that catalyzes the oxidative epoxidation of (S)-2-hydroxypropylphosphonate into (1R,2S)-epoxypropylphosphonate, the final step in the biosynthesis of fosfomycin antibiotic.<ref>PMID:16015285</ref> <ref>PMID:16186494</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zz/1zz7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zz7 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The 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.
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'''Crystal Structure of FeII HppE in Complex with Substrate form 1'''
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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<ref>PMID:16015285</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1zz7" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The 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.
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*[[Epoxidase 3D structures|Epoxidase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1ZZ7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_wedmorensis Streptomyces wedmorensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZZ7 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16015285 16015285]
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[[Category: Single protein]]
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[[Category: Streptomyces wedmorensis]]
[[Category: Streptomyces wedmorensis]]
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[[Category: Drennan, C L.]]
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[[Category: Drennan CL]]
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[[Category: Higgins, L J.]]
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[[Category: Higgins LJ]]
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[[Category: Liu, H W.]]
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[[Category: Liu HW]]
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[[Category: Liu, P.]]
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[[Category: Liu P]]
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[[Category: Yan, F.]]
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[[Category: Yan F]]
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[[Category: cupin]]
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[[Category: mononuclear iron enzyme]]
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[[Category: substrate-enzyme complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:43:35 2008''
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Current revision

Crystal Structure of FeII HppE in Complex with Substrate form 1

PDB ID 1zz7

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