2po5

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==Disease==
==Disease==
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Known disease associated with this structure: Protoporphyria, erythropoietic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=177000 177000]], Protoporphyria, erythropoietic, recessive, with liver failure OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=177000 177000]]
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Known disease associated with this structure: Protoporphyria, erythropoietic, autosomal dominant OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=612386 612386]], Protoporphyria, erythropoietic, autosomal recessive OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=612386 612386]]
==About this Structure==
==About this Structure==
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2PO5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA].
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2PO5 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA].
==Reference==
==Reference==
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Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis., Dailey HA, Wu CK, Horanyi P, Medlock AE, Najahi-Missaoui W, Burden AE, Dailey TA, Rose J, Biochemistry. 2007 Jul 10;46(27):7973-9. Epub 2007 Jun 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17567154 17567154]
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<ref group="xtra">PMID:17567154</ref><ref group="xtra">PMID:11175906</ref><ref group="xtra">PMID:10561552</ref><references group="xtra"/>
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The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis., Wu CK, Dailey HA, Rose JP, Burden A, Sellers VM, Wang BC, Nat Struct Biol. 2001 Feb;8(2):156-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11175906 11175906]
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Human ferrochelatase: crystallization, characterization of the [2Fe-2S] cluster and determination that the enzyme is a homodimer., Burden AE, Wu C, Dailey TA, Busch JL, Dhawan IK, Rose JP, Wang B, Dailey HA, Biochim Biophys Acta. 1999 Nov 16;1435(1-2):191-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10561552 10561552]
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[[Category: Ferrochelatase]]
[[Category: Ferrochelatase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
 
[[Category: Burden, A.]]
[[Category: Burden, A.]]
[[Category: Dailey, H A.]]
[[Category: Dailey, H A.]]
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[[Category: Protoheme]]
[[Category: Protoheme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:04:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 05:40:48 2009''

Revision as of 03:40, 17 February 2009

Image:2po5.png

Template:STRUCTURE 2po5

Contents

Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys

Template:ABSTRACT PUBMED 17567154

Disease

Known disease associated with this structure: Protoporphyria, erythropoietic, autosomal dominant OMIM:[612386], Protoporphyria, erythropoietic, autosomal recessive OMIM:[612386]

About this Structure

2PO5 is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Dailey HA, Wu CK, Horanyi P, Medlock AE, Najahi-Missaoui W, Burden AE, Dailey TA, Rose J. Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis. Biochemistry. 2007 Jul 10;46(27):7973-9. Epub 2007 Jun 14. PMID:17567154 doi:10.1021/bi700151f
  • Wu CK, Dailey HA, Rose JP, Burden A, Sellers VM, Wang BC. The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. Nat Struct Biol. 2001 Feb;8(2):156-60. PMID:11175906 doi:10.1038/84152
  • Burden AE, Wu C, Dailey TA, Busch JL, Dhawan IK, Rose JP, Wang B, Dailey HA. Human ferrochelatase: crystallization, characterization of the [2Fe-2S] cluster and determination that the enzyme is a homodimer. Biochim Biophys Acta. 1999 Nov 16;1435(1-2):191-7. PMID:10561552

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