1tkl: Difference between revisions
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Coproporphyrinogen_oxidase Coproporphyrinogen oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.3 1.3.3.3] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Coproporphyrinogen_oxidase Coproporphyrinogen oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.3 1.3.3.3] </span> | ||
|GENE= HEM13, YDR044W, YD5112.02 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= HEM13, YDR044W, YD5112.02 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1tk1|1TK1]], [[1tlb|1TLB]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tkl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tkl OCA], [http://www.ebi.ac.uk/pdbsum/1tkl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tkl RCSB]</span> | |||
}} | }} | ||
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[[Category: heme biosynthesis]] | [[Category: heme biosynthesis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:57:22 2008'' | ||
Revision as of 23:57, 30 March 2008
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| , resolution 2.00Å | |||||||
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| Gene: | HEM13, YDR044W, YD5112.02 (Saccharomyces cerevisiae) | ||||||
| Activity: | Coproporphyrinogen oxidase, with EC number 1.3.3.3 | ||||||
| Related: | 1TK1, 1TLB
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Yeast Oxygen-Dependent Coproporphyrinogen Oxidase
OverviewOverview
Coproporphyrinogen oxidase (CPO) is an essential enzyme that catalyzes the sixth step of the heme biosynthetic pathway. Unusually for heme biosynthetic enzymes, CPO exists in two evolutionarily and mechanistically distinct families, with eukaryotes and some prokaryotes employing members of the highly conserved oxygen-dependent CPO family. Here, we report the crystal structure of the oxygen-dependent CPO from Saccharomyces cerevisiae (Hem13p), which was determined by optimized sulfur anomalous scattering and refined to a resolution of 2.0 A. The protein adopts a novel structure that is quite different from predicted models and features a central flat seven-stranded anti-parallel sheet that is flanked by helices. The dimeric assembly, which is seen in different crystal forms, is formed by packing of helices and a short isolated strand that forms a beta-ladder with its counterpart in the partner subunit. The deep active-site cleft is lined by conserved residues and has been captured in open and closed conformations in two different crystal forms. A substratesized cavity is completely buried in the closed conformation by the approximately 8-A movement of a helix that forms a lid over the active site. The structure therefore suggests residues that likely play critical roles in catalysis and explains the deleterious effect of many of the mutations associated with the disease hereditary coproporphyria.
About this StructureAbout this Structure
1TKL is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the oxygen-dependant coproporphyrinogen oxidase (Hem13p) of Saccharomyces cerevisiae., Phillips JD, Whitby FG, Warby CA, Labbe P, Yang C, Pflugrath JW, Ferrara JD, Robinson H, Kushner JP, Hill CP, J Biol Chem. 2004 Sep 10;279(37):38960-8. Epub 2004 Jun 12. PMID:15194705
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