1u9m
From Proteopedia
(New page: 200px<br /><applet load="1u9m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u9m, resolution 2.00Å" /> '''Crystal structure of...) |
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| - | [[Image:1u9m.gif|left|200px]]<br /><applet load="1u9m" size=" | + | [[Image:1u9m.gif|left|200px]]<br /><applet load="1u9m" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1u9m, resolution 2.00Å" /> | caption="1u9m, resolution 2.00Å" /> | ||
'''Crystal structure of F58W mutant of cytochrome b5'''<br /> | '''Crystal structure of F58W mutant of cytochrome b5'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phe58 of cytochrome b5 is involved in stacking interactions with heme and | + | Phe58 of cytochrome b5 is involved in stacking interactions with heme and the axial ligand His63. To elucidate the contribution of the stacking interactions to protein stability, the crystal structures of the F58Y and F58W mutants were determined at high resolution. The structure of the F58Y mutant is basically the same as that of the wild-type protein. However, the mutation from Phe58 to Trp58 leads to difficulty in growing single crystals and results in a space-group change; the six molecules in the asymmetric unit form two groups that are related by a non-crystallographic twofold axis. The structure of F58W was determined using molecular replacement by making use of the non-crystallographic symmetry. The F58W mutation gives rise to multiple conformations of six side chains, a peptide linking two of the six residues and the extended propionic acid of the heme. The six molecules in the asymmetric unit of the F58W mutant structure are grouped into two types based on their conformations and one of the six molecules exhibits dual conformations. The stacking interactions are weakened owing to the increase/decrease of the angles between the indole ring of Trp58 and the His63/heme rings, which accounts for the lower stability of F58W compared with the wild-type protein. |
==About this Structure== | ==About this Structure== | ||
| - | 1U9M 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]. Full crystallographic information is available from [http:// | + | 1U9M 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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U9M 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: Lu, J | + | [[Category: Lu, J X.]] |
[[Category: Shan, L.]] | [[Category: Shan, L.]] | ||
| - | [[Category: Wang, Y | + | [[Category: Wang, Y H.]] |
| - | [[Category: Xia, Z | + | [[Category: Xia, Z X.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: aromatic-aromatic interactions]] | [[Category: aromatic-aromatic interactions]] | ||
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[[Category: structure-function relationship]] | [[Category: structure-function relationship]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:22:03 2008'' |
Revision as of 13:22, 21 February 2008
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Crystal structure of F58W mutant of cytochrome b5
Overview
Phe58 of cytochrome b5 is involved in stacking interactions with heme and the axial ligand His63. To elucidate the contribution of the stacking interactions to protein stability, the crystal structures of the F58Y and F58W mutants were determined at high resolution. The structure of the F58Y mutant is basically the same as that of the wild-type protein. However, the mutation from Phe58 to Trp58 leads to difficulty in growing single crystals and results in a space-group change; the six molecules in the asymmetric unit form two groups that are related by a non-crystallographic twofold axis. The structure of F58W was determined using molecular replacement by making use of the non-crystallographic symmetry. The F58W mutation gives rise to multiple conformations of six side chains, a peptide linking two of the six residues and the extended propionic acid of the heme. The six molecules in the asymmetric unit of the F58W mutant structure are grouped into two types based on their conformations and one of the six molecules exhibits dual conformations. The stacking interactions are weakened owing to the increase/decrease of the angles between the indole ring of Trp58 and the His63/heme rings, which accounts for the lower stability of F58W compared with the wild-type protein.
About this Structure
1U9M is a Single protein structure of sequence from Bos taurus with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the F58W mutant of cytochrome b5: the mutation leads to multiple conformations and weakens stacking interactions., Shan L, Lu JX, Gan JH, Wang YH, Huang ZX, Xia ZX, Acta Crystallogr D Biol Crystallogr. 2005 Feb;61(Pt 2):180-9. Epub 2005, Jan 19. PMID:15681869
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