1olt

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[[Image:1olt.jpg|left|200px]]
[[Image:1olt.jpg|left|200px]]
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{{Structure
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|PDB= 1olt |SIZE=350|CAPTION= <scene name='initialview01'>1olt</scene>, resolution 2.07&Aring;
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The line below this paragraph, containing "STRUCTURE_1olt", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Sam+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>
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{{STRUCTURE_1olt| PDB=1olt | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1olt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1olt OCA], [http://www.ebi.ac.uk/pdbsum/1olt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1olt RCSB]</span>
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'''COPROPORPHYRINOGEN III OXIDASE (HEMN) FROM ESCHERICHIA COLI IS A RADICAL SAM ENZYME.'''
'''COPROPORPHYRINOGEN III OXIDASE (HEMN) FROM ESCHERICHIA COLI IS A RADICAL SAM ENZYME.'''
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[[Category: Schubert, W D.]]
[[Category: Schubert, W D.]]
[[Category: 4fe-4s cluster]]
[[Category: 4fe-4s cluster]]
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[[Category: decarboxylase]]
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[[Category: Decarboxylase]]
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[[Category: heme biosynthesis]]
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[[Category: Heme biosynthesis]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: radical sam enzyme]]
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[[Category: Radical sam enzyme]]
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[[Category: s-adenosyl-l-methionine]]
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[[Category: S-adenosyl-l-methionine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:00:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:47:04 2008''
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Revision as of 01:00, 3 May 2008

Image:1olt.jpg

Template:STRUCTURE 1olt

COPROPORPHYRINOGEN III OXIDASE (HEMN) FROM ESCHERICHIA COLI IS A RADICAL SAM ENZYME.


Overview

'Radical SAM' enzymes generate catalytic radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. We present the first crystal structure of a Radical SAM enzyme, that of HemN, the Escherichia coli oxygen-independent coproporphyrinogen III oxidase, at 2.07 A resolution. HemN catalyzes the essential conversion of coproporphyrinogen III to protoporphyrinogen IX during heme biosynthesis. HemN binds a 4Fe-4S cluster through three cysteine residues conserved in all Radical SAM enzymes. A juxtaposed SAM coordinates the fourth Fe ion through its amide nitrogen and carboxylate oxygen. The SAM sulfonium sulfur is near both the Fe (3.5 A) and a neighboring sulfur of the cluster (3.6 A), allowing single electron transfer from the 4Fe-4S cluster to the SAM sulfonium. SAM is cleaved yielding a highly oxidizing 5'-deoxyadenosyl radical. HemN, strikingly, binds a second SAM immediately adjacent to the first. It may thus successively catalyze two propionate decarboxylations. The structure of HemN reveals the cofactor geometry required for Radical SAM catalysis and sets the stage for the development of inhibitors with antibacterial function due to the uniquely bacterial occurrence of the enzyme.

About this Structure

1OLT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes., Layer G, Moser J, Heinz DW, Jahn D, Schubert WD, EMBO J. 2003 Dec 1;22(23):6214-24. PMID:14633981 Page seeded by OCA on Sat May 3 04:00:33 2008

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