2hrc: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: left|200px<br /> <applet load="2hrc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hrc, resolution 1.70Å" /> '''1.7 angstrom struct... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2hrc. | [[Image:2hrc.jpg|left|200px]]<br /><applet load="2hrc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2hrc" size=" | |||
caption="2hrc, resolution 1.70Å" /> | caption="2hrc, resolution 1.70Å" /> | ||
'''1.7 angstrom structure of human ferrochelatase variant R115L'''<br /> | '''1.7 angstrom structure of human ferrochelatase variant R115L'''<br /> | ||
| Line 6: | Line 5: | ||
==Overview== | ==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. | 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. | ||
==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 CL, FES, IMD, CHD and GOL 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:// | 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]. | ||
==Reference== | ==Reference== | ||
| Line 33: | Line 29: | ||
[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:37:46 2008'' | ||
