2hrc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2hrc.jpg|left|200px]]<br /><applet load="2hrc" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2hrc.jpg|left|200px]]
-
caption="2hrc, resolution 1.70&Aring;" />
+
 
-
'''1.7 angstrom structure of human ferrochelatase variant R115L'''<br />
+
{{Structure
 +
|PDB= 2hrc |SIZE=350|CAPTION= <scene name='initialview01'>2hrc</scene>, resolution 1.70&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
 +
|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]
 +
|GENE= FECH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
 +
}}
 +
 
 +
'''1.7 angstrom structure of human ferrochelatase variant R115L'''
 +
 
==Overview==
==Overview==
Line 10: Line 19:
==About this Structure==
==About this Structure==
-
2HRC 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=CL:'>CL</scene>, <scene name='pdbligand=FES:'>FES</scene>, <scene name='pdbligand=IMD:'>IMD</scene>, <scene name='pdbligand=CHD:'>CHD</scene> and <scene name='pdbligand=GOL:'>GOL</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=2HRC OCA].
+
2HRC 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=2HRC OCA].
==Reference==
==Reference==
-
Substrate interactions with human ferrochelatase., Medlock A, Swartz L, Dailey TA, Dailey HA, Lanzilotta WN, Proc Natl Acad Sci U S A. 2007 Feb 6;104(6):1789-93. Epub 2007 Jan 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17261801 17261801]
+
Substrate interactions with human ferrochelatase., Medlock A, Swartz L, Dailey TA, Dailey HA, Lanzilotta WN, Proc Natl Acad Sci U S A. 2007 Feb 6;104(6):1789-93. Epub 2007 Jan 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17261801 17261801]
[[Category: Ferrochelatase]]
[[Category: Ferrochelatase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
Line 32: Line 41:
[[Category: x-ray crystallography]]
[[Category: x-ray crystallography]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:44:52 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:20:35 2008''

Revision as of 15:20, 20 March 2008

Image:2hrc.jpg


PDB ID 2hrc

Drag the structure with the mouse to rotate
, resolution 1.70Å
Ligands: , , , and
Gene: FECH (Homo sapiens)
Activity: Ferrochelatase, with EC number 4.99.1.1
Coordinates: save as pdb, mmCIF, xml



1.7 angstrom structure of human ferrochelatase variant R115L


Contents

Overview

Ferrochelatase, the terminal enzyme in heme biosynthesis, catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme IX. Human ferrochelatase is a homodimeric, inner mitochondrial membrane-associated enzyme that possesses an essential [2Fe-2S] cluster. In this work, we report the crystal structure of human ferrochelatase with the substrate protoporphyrin IX bound as well as a higher resolution structure of the R115L variant without bound substrate. The data presented reveal that the porphyrin substrate is bound deep within an enclosed pocket. When compared with the location of N-methylmesoporphyrin in the Bacillus subtilis ferrochelatase, the porphyrin is rotated by approximately 100 degrees and is buried an additional 4.5 A deeper within the active site. The propionate groups of the substrate do not protrude into solvent and are bound in a manner similar to what has been observed in uroporphyrinogen decarboxylase. Furthermore, in the substrate-bound form, the jaws of the active site mouth are closed so that the porphyrin substrate is completely engulfed in the pocket. These data provide insights that will aid in the determination of the mechanism for ferrochelatase.

Disease

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

About this Structure

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

Reference

Substrate interactions with human ferrochelatase., Medlock A, Swartz L, Dailey TA, Dailey HA, Lanzilotta WN, Proc Natl Acad Sci U S A. 2007 Feb 6;104(6):1789-93. Epub 2007 Jan 29. PMID:17261801

Page seeded by OCA on Thu Mar 20 17:20:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hrc"
Personal tools