2qd1

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[[Image:2qd1.gif|left|200px]]<br /><applet load="2qd1" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2qd1.gif|left|200px]]
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caption="2qd1, resolution 2.20&Aring;" />
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'''2.2 Angstrom Structure of the human ferrochelatase variant E343K with substrate bound'''<br />
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{{Structure
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|PDB= 2qd1 |SIZE=350|CAPTION= <scene name='initialview01'>2qd1</scene>, resolution 2.20&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=PP9:PROTOPORPHYRIN+IX'>PP9</scene>, <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene> and <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1]
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|GENE= FECH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''2.2 Angstrom Structure of the human ferrochelatase variant E343K with substrate bound'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2QD1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FES:'>FES</scene>, <scene name='pdbligand=PP9:'>PP9</scene>, <scene name='pdbligand=CHD:'>CHD</scene> and <scene name='pdbligand=IMD:'>IMD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QD1 OCA].
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2QD1 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=2QD1 OCA].
==Reference==
==Reference==
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A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase., Medlock AE, Dailey TA, Ross TA, Dailey HA, Lanzilotta WN, J Mol Biol. 2007 Nov 2;373(4):1006-16. Epub 2007 Aug 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17884090 17884090]
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A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase., Medlock AE, Dailey TA, Ross TA, Dailey HA, Lanzilotta WN, J Mol Biol. 2007 Nov 2;373(4):1006-16. Epub 2007 Aug 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17884090 17884090]
[[Category: Ferrochelatase]]
[[Category: Ferrochelatase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: protopophyrin ix]]
[[Category: protopophyrin ix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:38:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:24:32 2008''

Revision as of 16:24, 20 March 2008

Image:2qd1.gif


PDB ID 2qd1

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands: , , and
Gene: FECH (Homo sapiens)
Activity: Ferrochelatase, with EC number 4.99.1.1
Coordinates: save as pdb, mmCIF, xml



2.2 Angstrom Structure of the human ferrochelatase variant E343K with substrate bound


Contents

Overview

Ferrochelatase (protoheme ferrolyase, EC 4.99.1.1) is the terminal enzyme in heme biosynthesis and catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme IX (heme). Due to the many critical roles of heme, synthesis of heme is required by the vast majority of organisms. Despite significant investigation of both the microbial and eukaryotic enzyme, details of metal chelation remain unidentified. Here we present the first structure of the wild-type human enzyme, a lead-inhibited intermediate of the wild-type enzyme with bound metallated porphyrin macrocycle, the product bound form of the enzyme, and a higher resolution model for the substrate-bound form of the E343K variant. These data paint a picture of an enzyme that undergoes significant changes in secondary structure during the catalytic cycle. The role that these structural alterations play in overall catalysis and potential protein-protein interactions with other proteins, as well as the possible molecular basis for these changes, is discussed. The atomic details and structural rearrangements presented herein significantly advance our understanding of the substrate binding mode of ferrochelatase and reveal new conformational changes in a structurally conserved pi-helix that is predicted to have a central role in product release.

Disease

Known diseases associated with this structure: Protoporphyria, erythropoietic OMIM:[177000], Protoporphyria, erythropoietic, recessive, with liver failure OMIM:[177000]

About this Structure

2QD1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase., Medlock AE, Dailey TA, Ross TA, Dailey HA, Lanzilotta WN, J Mol Biol. 2007 Nov 2;373(4):1006-16. Epub 2007 Aug 23. PMID:17884090

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