1f9b: Difference between revisions
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New page: left|200px<br /><applet load="1f9b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f9b, resolution 2.7Å" /> '''MELANIN PROTEIN INTER... |
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[[Image:1f9b.gif|left|200px]]<br /><applet load="1f9b" size=" | [[Image:1f9b.gif|left|200px]]<br /><applet load="1f9b" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1f9b, resolution 2.7Å" /> | caption="1f9b, resolution 2.7Å" /> | ||
'''MELANIN PROTEIN INTERACTION: X-RAY STRUCTURE OF THE COMPLEX OF MARE LACTOFERRIN WITH MELANIN MONOMERS'''<br /> | '''MELANIN PROTEIN INTERACTION: X-RAY STRUCTURE OF THE COMPLEX OF MARE LACTOFERRIN WITH MELANIN MONOMERS'''<br /> | ||
==Overview== | ==Overview== | ||
The concentration of melanin determines the intensity of colors of the | The concentration of melanin determines the intensity of colors of the skin and hair of animals. Melanin pigments are tyrosine-based polymers formed in melanocytes within specialized organelles called melanosomes. In order to understand the mechanism of melanin polymerization, lactoferrin, a basic protein with a pI value of 9.0, has been used to produce melanin. Lactoferrin is a monomeric iron-binding protein with a molecular weight of 80 kDa. The crystals of lactoferrin were soaked in a solution containing dihydroxyphenylalanine (DOPA) and tyrosinase enzyme. These crystals were used for X-ray intensity data collection. The intensity data were collected to 2.7-A resolution to an overall completeness of 91% with an R(sym) of 0.071. The crystals belong to orthorhombic space group P2(1)2(1)2(1) with cell dimensions: a = 85.0 A, b = 99.8 A, c = 103.4 A. The structure was determined by molecular replacement method, using the model of diferric mare lactoferrin, and refined to an R-factor 0.215 (R(free) = 0.287) for all the data to 2.7-A resolution. The final model comprises 5,281 protein atoms from 689 amino acids, 2Fe(3+), 2CO(2-)(3) ions, 2 indole-5,6-quinone molecules (IQ), and 73 water molecules. Two IQ molecules, one in each lobe, bind to lactoferrin. In the C-lobe, the IQ binds in the iron-binding cleft, whereas in the N-lobe, it is located in the side pocket between two alpha-helices, filled with solvent molecules in the native iron-saturated mare lactoferrin. The IQ molecules interact with protein molecule mainly through glutamic acid in both lobes, without significant perturbation to the protein structure. The orientation of N- and C-lobes in the present structure is similar to that observed in the native iron-saturated protein. However, as a result of the binding of IQ molecules, the orientations of the domains N1, N2 and C1, C2 in the two cases differ slightly. | ||
==About this Structure== | ==About this Structure== | ||
1F9B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with FE, BCT and 3ID as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1F9B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=BCT:'>BCT</scene> and <scene name='pdbligand=3ID:'>3ID</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F9B OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Kumar, S.]] | [[Category: Kumar, S.]] | ||
[[Category: Raman, G.]] | [[Category: Raman, G.]] | ||
[[Category: Sharma, A | [[Category: Sharma, A K.]] | ||
[[Category: Singh, N.]] | [[Category: Singh, N.]] | ||
[[Category: Singh, T | [[Category: Singh, T P.]] | ||
[[Category: 3ID]] | [[Category: 3ID]] | ||
[[Category: BCT]] | [[Category: BCT]] | ||
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[[Category: metal-binding]] | [[Category: metal-binding]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:14 2008'' | ||