3sch

From Proteopedia

(Difference between revisions)

Current revision

Co(II)-HppE with R-HPP

Structural highlights

3sch is a 2 chain structure with sequence from Streptomyces wedmorensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2]

Publication Abstract from PubMed

Hydroxypropylphosphonic acid epoxidase (HppE) is an unusual mononuclear iron enzyme that uses dioxygen to catalyze the oxidative epoxidation of (S)-2-hydroxypropylphosphonic acid (S-HPP) in the biosynthesis of the antibiotic fosfomycin. Additionally, the enzyme converts the R-enantiomer of the substrate (R-HPP) to 2-oxo-propylphosphonic acid. To probe the mechanism of HppE regiospecificity, we determined three X-ray structures: R-HPP with inert cobalt-containing enzyme (Co(II)-HppE) at 2.1 A resolution; R-HPP with active iron-containing enzyme (Fe(II)-HppE) at 3.0 A resolution; and S-HPP-Fe(II)-HppE in complex with dioxygen mimic NO at 2.9 A resolution. These structures, along with previously determined structures of S-HPP-HppE, identify the dioxygen binding site on iron and elegantly illustrate how HppE is able to recognize both substrate enantiomers to catalyze two completely distinct reactions.

Structural Basis of Regiospecificity of a Mononuclear Iron Enzyme in Antibiotic Fosfomycin Biosynthesis.,Yun D, Dey M, Higgins LJ, Yan F, Liu HW, Drennan CL J Am Chem Soc. 2011 Jun 30. PMID:21682308^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Higgins LJ, Yan F, Liu P, Liu HW, Drennan CL. Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme. Nature. 2005 Oct 6;437(7060):838-44. Epub 2005 Jul 13. PMID:16015285 doi:http://dx.doi.org/10.1038/nature03924
↑ McLuskey K, Cameron S, Hammerschmidt F, Hunter WN. Structure and reactivity of hydroxypropylphosphonic acid epoxidase in fosfomycin biosynthesis by a cation- and flavin-dependent mechanism. Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14221-6. Epub 2005 Sep 26. PMID:16186494
↑ Yun D, Dey M, Higgins LJ, Yan F, Liu HW, Drennan CL. Structural Basis of Regiospecificity of a Mononuclear Iron Enzyme in Antibiotic Fosfomycin Biosynthesis. J Am Chem Soc. 2011 Jun 30. PMID:21682308 doi:10.1021/ja2025728

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3sch"

Categories: Large Structures | Streptomyces wedmorensis | Drennan CL

@@ Line 1: / Line 1: @@
-[[Image:3sch.png|left|200px]]
-<!--
+==Co(II)-HppE with R-HPP==
-The line below this paragraph, containing "STRUCTURE_3sch", creates the "Structure Box" on the page.
+<StructureSection load='3sch' size='340' side='right'caption='[[3sch]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3sch]] 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=3SCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SCH FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TB6:[(2R)-2-HYDROXYPROPYL]PHOSPHONIC+ACID'>TB6</scene></td></tr>
-{{STRUCTURE_3sch|  PDB=3sch  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sch OCA], [https://pdbe.org/3sch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sch RCSB], [https://www.ebi.ac.uk/pdbsum/3sch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sch ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Hydroxypropylphosphonic acid epoxidase (HppE) is an unusual mononuclear iron enzyme that uses dioxygen to catalyze the oxidative epoxidation of (S)-2-hydroxypropylphosphonic acid (S-HPP) in the biosynthesis of the antibiotic fosfomycin. Additionally, the enzyme converts the R-enantiomer of the substrate (R-HPP) to 2-oxo-propylphosphonic acid. To probe the mechanism of HppE regiospecificity, we determined three X-ray structures: R-HPP with inert cobalt-containing enzyme (Co(II)-HppE) at 2.1 A resolution; R-HPP with active iron-containing enzyme (Fe(II)-HppE) at 3.0 A resolution; and S-HPP-Fe(II)-HppE in complex with dioxygen mimic NO at 2.9 A resolution. These structures, along with previously determined structures of S-HPP-HppE, identify the dioxygen binding site on iron and elegantly illustrate how HppE is able to recognize both substrate enantiomers to catalyze two completely distinct reactions.
-===Co(II)-HppE with R-HPP===
+Structural Basis of Regiospecificity of a Mononuclear Iron Enzyme in Antibiotic Fosfomycin Biosynthesis.,Yun D, Dey M, Higgins LJ, Yan F, Liu HW, Drennan CL J Am Chem Soc. 2011 Jun 30. PMID:21682308<ref>PMID:21682308</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3sch" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_21682308}}, adds the Publication Abstract to the page
+*[[Epoxidase 3D structures|Epoxidase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 21682308 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21682308}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[3sch]] is a 2 chain structure with 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=3SCH OCA].
-==Reference==
-<ref group="xtra">PMID:021682308</ref><references group="xtra"/>
 [[Category: Streptomyces wedmorensis]]
-[[Category: Drennan, C L.]]
+[[Category: Drennan CL]]
-[[Category: Cupin-fold]]
-[[Category: Hydroxypropylphosphonic acid epoxidase]]
-[[Category: Metal binding protein]]
-[[Category: Mononuclear non-heme iron]]

3sch

From Proteopedia

Current revision

Co(II)-HppE with R-HPP

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox