1c9e

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(Difference between revisions)

Revision as of 08:03, 29 November 2017

STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE

Structural highlights

1c9e is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1ak1, 1c1h
Activity:	Ferrochelatase, with EC number 4.99.1.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HEMH_BACSU] Catalyzes the ferrous insertion into protoporphyrin IX.

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

Ferrochelatase, the enzyme catalyzing metallation of protoporphyrin IX at the terminal step of heme biosynthesis, was co-crystallized with an isomer mixture of the potent inhibitor N-methylmesoporphyrin (N-MeMP). The X-ray structure revealed the active site of the enzyme, to which only one of the isomers was bound, and for the first time allowed characterization of the mode of porphyrin macrocycle distortion by ferrochelatase. Crystallization of ferrochelatase and N-MeMP in the presence of Cu(2+) leads to metallation and demethylation of N-MeMP. A mechanism of porphyrin distortion is proposed, which assumes that the enzyme holds pyrrole rings B, C and D in a vice-like grip and forces a 36 degrees tilt on ring A.

Structural and mechanistic basis of porphyrin metallation by ferrochelatase.,Lecerof D, Fodje M, Hansson A, Hansson M, Al-Karadaghi S J Mol Biol. 2000 Mar 17;297(1):221-32. PMID:10704318^[1]

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

References

↑ Lecerof D, Fodje M, Hansson A, Hansson M, Al-Karadaghi S. Structural and mechanistic basis of porphyrin metallation by ferrochelatase. J Mol Biol. 2000 Mar 17;297(1):221-32. PMID:10704318 doi:10.1006/jmbi.2000.3569

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/1c9e"

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE==
 <StructureSection load='1c9e' size='340' side='right' caption='[[1c9e]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1c9e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C9E FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1c9e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C9E FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MP1:N-METHYLMESOPORPHYRIN+CONTAINING+COPPER'>MP1</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ak1|1ak1]], [[1c1h|1c1h]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </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=1c9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9e OCA], [http://pdbe.org/1c9e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c9e RCSB], [http://www.ebi.ac.uk/pdbsum/1c9e 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=1c9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9e OCA], [http://pdbe.org/1c9e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c9e RCSB], [http://www.ebi.ac.uk/pdbsum/1c9e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1c9e ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1c9e" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Ferrochelatase|Ferrochelatase]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus globigii migula 1900]]
+[[Category: Vibrio subtilis ehrenberg 1835]]
 [[Category: Ferrochelatase]]
 [[Category: Al-Karadaghi, S]]

1c9e

From Proteopedia

Revision as of 08:03, 29 November 2017

STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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