1es1
From Proteopedia
(New page: 200px<br /><applet load="1es1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1es1, resolution 2.10Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1es1.jpg|left|200px]]<br /><applet load="1es1" size=" | + | [[Image:1es1.jpg|left|200px]]<br /><applet load="1es1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1es1, resolution 2.10Å" /> | caption="1es1, resolution 2.10Å" /> | ||
'''CRYSTAL STRUCTURE OF VAL61HIS MUTANT OF TRYPSIN-SOLUBILIZED FRAGMENT OF CYTOCHROME B5'''<br /> | '''CRYSTAL STRUCTURE OF VAL61HIS MUTANT OF TRYPSIN-SOLUBILIZED FRAGMENT OF CYTOCHROME B5'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the recombinant trypsin-solubilized fragment of | + | The crystal structure of the recombinant trypsin-solubilized fragment of the microsomal cytochrome b(5) from bovine liver has been determined at 1.9 A resolution and compared with the reported crystal structure of the lipase-solubilized fragment of the membrane protein cytochrome b(5). The two structures are similar to each other. However, some detailed structural differences are observed: the conformation of the segment Asn16-Ser20 is quite different, some helices around the heme and some segments between the helices are shifted slightly, the heme is rotated about the normal of the mean plane of heme, one of the propionates of the heme exhibits a different conformation. The average coordination distances between the iron and the two nitrogen atoms of the imidazole ligands are the same in the two structures. Most of the structural differences can be attributed to the different intermolecular interactions which result from the crystal packing. The wild-type protein structure is also compared with its Val61His mutant, showing that the heme binding and the main chain conformations are basically identical with each other except for the local area of the mutation site. However, when Val61 is mutated to histidine, the large side chain of His61 is forced to point away from the heme pocket toward the solvent region, disturbing the micro-environment of the heme pocket and influencing the stability and the redox potential of the protein. |
==About this Structure== | ==About this Structure== | ||
| - | 1ES1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 1ES1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1QDX. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ES1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gan, J | + | [[Category: Gan, J H.]] |
| - | [[Category: Huang, Z | + | [[Category: Huang, Z X.]] |
| - | [[Category: Wang, W | + | [[Category: Wang, W H.]] |
| - | [[Category: Wang, Y | + | [[Category: Wang, Y H.]] |
[[Category: Wu, J.]] | [[Category: Wu, J.]] | ||
| - | [[Category: Xia, Z | + | [[Category: Xia, Z X.]] |
[[Category: Xie, Y.]] | [[Category: Xie, Y.]] | ||
| - | [[Category: Xue, L | + | [[Category: Xue, L L.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: cytochrome b5; trypsin-cleaved fragment; mutant val61his;crystal structure; structure comparison with the wild type fragment;]] | [[Category: cytochrome b5; trypsin-cleaved fragment; mutant val61his;crystal structure; structure comparison with the wild type fragment;]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:54 2008'' |
Revision as of 10:30, 21 February 2008
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CRYSTAL STRUCTURE OF VAL61HIS MUTANT OF TRYPSIN-SOLUBILIZED FRAGMENT OF CYTOCHROME B5
Overview
The crystal structure of the recombinant trypsin-solubilized fragment of the microsomal cytochrome b(5) from bovine liver has been determined at 1.9 A resolution and compared with the reported crystal structure of the lipase-solubilized fragment of the membrane protein cytochrome b(5). The two structures are similar to each other. However, some detailed structural differences are observed: the conformation of the segment Asn16-Ser20 is quite different, some helices around the heme and some segments between the helices are shifted slightly, the heme is rotated about the normal of the mean plane of heme, one of the propionates of the heme exhibits a different conformation. The average coordination distances between the iron and the two nitrogen atoms of the imidazole ligands are the same in the two structures. Most of the structural differences can be attributed to the different intermolecular interactions which result from the crystal packing. The wild-type protein structure is also compared with its Val61His mutant, showing that the heme binding and the main chain conformations are basically identical with each other except for the local area of the mutation site. However, when Val61 is mutated to histidine, the large side chain of His61 is forced to point away from the heme pocket toward the solvent region, disturbing the micro-environment of the heme pocket and influencing the stability and the redox potential of the protein.
About this Structure
1ES1 is a Single protein structure of sequence from Bos taurus with as ligand. This structure supersedes the now removed PDB entry 1QDX. Full crystallographic information is available from OCA.
Reference
Crystal structure of recombinant trypsin-solubilized fragment of cytochrome b(5) and the structural comparison with Val61His mutant., Wu J, Gan JH, Xia ZX, Wang YH, Wang WH, Xue LL, Xie Y, Huang ZX, Proteins. 2000 Aug 1;40(2):249-57. PMID:10842340
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