This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1rxf

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:23, 22 September 2021

DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH FE(II)

Structural highlights

1rxf is a 1 chain structure with sequence from As 4.1611. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CEFE_STRC2] Catalyzes the step from penicillin N to deacetoxy-cephalosporin C.

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 PubMed

Penicillins and cephalosporins are among the most widely used therapeutic agents. These antibiotics are produced from fermentation-derived materials as their chemical synthesis is not commercially viable. Unconventional steps in their biosynthesis are catalysed by Fe(II)-dependent oxidases/oxygenases; isopenicillin N synthase (IPNS) creates in one step the bicyclic nucleus of penicillins, and deacetoxycephalosporin C synthase (DAOCS) catalyses the expansion of the penicillin nucleus into the nucleus of cephalosporins. Both enzymes use dioxygen-derived ferryl intermediates in catalysis but, in contrast to IPNS, the ferryl form of DAOCS is produced by the oxidative splitting of a co-substrate, 2-oxoglutarate (alpha-ketoglutarate). This route of controlled ferryl formation and reaction is common to many mononuclear ferrous enzymes, which participate in a broader range of reactions than their well-characterized counterparts, the haem enzymes. Here we report the first crystal structure of a 2-oxoacid-dependent oxygenase. High-resolution structures for apo-DAOCS, the enzyme complexed with Fe(II), and with Fe(II) and 2-oxoglutarate, were obtained from merohedrally twinned crystals. Using a model based on these structures, we propose a mechanism for ferryl formation.

Structure of a cephalosporin synthase.,Valegard K, van Scheltinga AC, Lloyd MD, Hara T, Ramaswamy S, Perrakis A, Thompson A, Lee HJ, Baldwin JE, Schofield CJ, Hajdu J, Andersson I Nature. 1998 Aug 20;394(6695):805-9. PMID:9723623^[1]

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

References

↑ Valegard K, van Scheltinga AC, Lloyd MD, Hara T, Ramaswamy S, Perrakis A, Thompson A, Lee HJ, Baldwin JE, Schofield CJ, Hajdu J, Andersson I. Structure of a cephalosporin synthase. Nature. 1998 Aug 20;394(6695):805-9. PMID:9723623 doi:http://dx.doi.org/10.1038/29575

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rxf"

@@ Line 3: / Line 3: @@
 <StructureSection load='1rxf' size='340' side='right'caption='[[1rxf]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1rxf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1611 As 4.1611]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RXF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RXF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1rxf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/As_4.1611 As 4.1611]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RXF FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=1rxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rxf OCA], [http://pdbe.org/1rxf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rxf RCSB], [http://www.ebi.ac.uk/pdbsum/1rxf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rxf ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rxf OCA], [https://pdbe.org/1rxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rxf RCSB], [https://www.ebi.ac.uk/pdbsum/1rxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rxf ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CEFE_STRC2 CEFE_STRC2]] Catalyzes the step from penicillin N to deacetoxy-cephalosporin C.
+[[https://www.uniprot.org/uniprot/CEFE_STRC2 CEFE_STRC2]] Catalyzes the step from penicillin N to deacetoxy-cephalosporin C.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1rxf

From Proteopedia

Revision as of 07:23, 22 September 2021

DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH FE(II)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox