2po5

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{{STRUCTURE_2po5| PDB=2po5 | SCENE= }}
{{STRUCTURE_2po5| PDB=2po5 | SCENE= }}
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'''Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys'''
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===Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys===
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==Overview==
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Ferrochelatase catalyzes the terminal step in heme biosynthesis, the insertion of ferrous iron into protoporphyrin to form protoheme IX. The crystal structures of human ferrochelatase both with and without the protoporphyrin substrate bound have been determined previously. The substrate-free enzyme has an open active site pocket, while in the substrate-bound enzyme, the active site pocket is closed around the porphyrin macrocycle and a number of active site residues have reoriented side chains. To understand how and why these structural changes occur, we have substituted three amino acid residues (H263, H341, and F337) whose side chains occupy different spatial positions in the substrate-free versus substrate-bound ferrochelatases. The catalytic and structural properties of ferrochelatases containing the amino acid substitutions H263C, H341C, and F337A were examined. It was found that in the H263C and H341C variants, but not the F337A variant enzymes, the side chains of N75, M76, R164, H263, F337, H341, and E343 are oriented in a fashion similar to what is found in ferrochelatase with the bound porphyrin substrate. However, all of the variant forms possess open active site pockets which are found in the structure of porphyrin-free ferrochelatase. Thus, while the interior walls of the active site pocket are remodeled in these variants, the exterior lips remain unaltered in position. One possible explanation for this collective reorganization of active site side chains is the presence of a hydrogen bond network among H263, H341, and E343. This network is disrupted in the variants by alteration of H263C or H341C. In the substrate-bound enzyme, the formation of a hydrogen bond between H263 and a pyrrole nitrogen results in disruption of the network. The possible role of this network in catalysis is discussed.
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(as it appears on PubMed at http://www.pubmed.gov), where 17567154 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17567154}}
==Disease==
==Disease==
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==Reference==
==Reference==
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]
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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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]
[[Category: Ferrochelatase]]
[[Category: Ferrochelatase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Proteolytically processed mitochondrial inner membrane protein]]
[[Category: Proteolytically processed mitochondrial inner membrane protein]]
[[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''

Revision as of 06:04, 28 July 2008

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 OMIM:[177000], Protoporphyria, erythropoietic, recessive, with liver failure OMIM:[177000]

About this Structure

2PO5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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:17567154

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:11175906

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:10561552

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