1olt: Difference between revisions
New page: left|200px<br /> <applet load="1olt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1olt, resolution 2.07Å" /> '''COPROPORPHYRINOGEN ... |
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==About this Structure== | ==About this Structure== | ||
1OLT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ ]] with SAM and SF4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OLT OCA]]. | 1OLT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with SAM and SF4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OLT OCA]]. | ||
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14633981 14633981] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14633981 14633981] | ||
[[Category: Escherichia coli]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Heinz, D.W.]] | [[Category: Heinz, D.W.]] | ||
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[[Category: s-adenosyl-l-methionine]] | [[Category: s-adenosyl-l-methionine]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:17:39 2007'' | ||
Revision as of 12:12, 30 October 2007
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COPROPORPHYRINOGEN III OXIDASE (HEMN) FROM ESCHERICHIA COLI IS A RADICAL SAM ENZYME.
OverviewOverview
'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 ... [(full description)]
About this StructureAbout this Structure
1OLT is a [Single protein] structure of sequence from [Escherichia coli] with SAM and SF4 as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
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
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