Sandbox Reserved 713: Difference between revisions
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<Structure load='2fkl' size='400' align='left' background='none' caption=' | <Structure load='2fkl' size='400' align='left' background='none' caption=' | ||
[[2fkl]]'/> | [[2fkl]]'/> | ||
===Secondary structure=== | |||
2fkl is constituted by two chains called A and B <ref name="MolecularI"/>. Both chains have the same length and the same organization. Each chain also contains an <scene name='Sandbox_Reserved_713/Helice_alpha/1'>alpha-helix</scene> going from residue 147 to 159 packed against a triple-strand beta sheet. The strand <scene name='Sandbox_Reserved_719/Beta1/1'>Beta1</scene> going from residue 133 to 139, the <scene name='Sandbox_Reserved_713/Beta_stream2/1'>Beta2</scene> going from residue 162 to 167, and the <scene name='Sandbox_Reserved_713/Beta_stream3/1'>Beta3</scene> going from residue 181 to 188. There is one more Beta sheet, <scene name='Sandbox_Reserved_713/Beta_0/1'>B0</scene>, formed by the residues 127 to 139 of the B chain. | 2fkl is constituted by two chains called A and B <ref name="MolecularI"/>. Both chains have the same length and the same organization. Each chain also contains an <scene name='Sandbox_Reserved_713/Helice_alpha/1'>alpha-helix</scene> going from residue 147 to 159 packed against a triple-strand beta sheet. The strand <scene name='Sandbox_Reserved_719/Beta1/1'>Beta1</scene> going from residue 133 to 139, the <scene name='Sandbox_Reserved_713/Beta_stream2/1'>Beta2</scene> going from residue 162 to 167, and the <scene name='Sandbox_Reserved_713/Beta_stream3/1'>Beta3</scene> going from residue 181 to 188. There is one more Beta sheet, <scene name='Sandbox_Reserved_713/Beta_0/1'>B0</scene>, formed by the residues 127 to 139 of the B chain. | ||
===Tertiary structure=== | |||
The three dimensional structure of the Cu-Binding Domain was first determined by resonance multidimensional NMR spectroscopy <ref name="MolecularI"> PMID:12611883 </ref>. More recently, the determination of the crystallographic structure permits to define the molecular interaction between the Cu-Binding Domain and copper.<ref name="Molecular" /> | |||
Between the Cysteine 133 and the Cystein 187 we can find a <scene name='Sandbox_Reserved_719/Disulfide_bond/1'>disulfide bound</scene> which links <scene name='Sandbox_Reserved_713/Disulfide_brige_beta1_3/1'>the strand beta 1 and beta 3</scene> and <scene name='Sandbox_Reserved_713/Bislufide_bridge/1'>another one</scene> between cystein 158 and cystein186 which links the alpha helix to the strand Beta 3. Between the cysteine 144 and the cysteine 174 we can describe another <scene name='Sandbox_Reserved_713/Dislfide_brige_2/1'>disulfide bound</scene>. | Between the Cysteine 133 and the Cystein 187 we can find a <scene name='Sandbox_Reserved_719/Disulfide_bond/1'>disulfide bound</scene> which links <scene name='Sandbox_Reserved_713/Disulfide_brige_beta1_3/1'>the strand beta 1 and beta 3</scene> and <scene name='Sandbox_Reserved_713/Bislufide_bridge/1'>another one</scene> between cystein 158 and cystein186 which links the alpha helix to the strand Beta 3. Between the cysteine 144 and the cysteine 174 we can describe another <scene name='Sandbox_Reserved_713/Dislfide_brige_2/1'>disulfide bound</scene>. | ||
In order to improve the stabilization of this structure there is a small <scene name='Sandbox_Reserved_713/Hydrophobic_core/1'>hydrophobic core</scene> which contain different residues from each seconday structure. (Leu 136, Trp 150, Val 153, Ala154, Leu 165, Met 170, Val 182 and Val 185) | In order to improve the stabilization of this structure there is a small <scene name='Sandbox_Reserved_713/Hydrophobic_core/1'>hydrophobic core</scene> which contain different residues from each seconday structure. (Leu 136, Trp 150, Val 153, Ala154, Leu 165, Met 170, Val 182 and Val 185) | ||
The study of the structure also showed on the surface of the Cu-Binding Site different regions <scene name='Sandbox_Reserved_713/Negatively_charged/1'>highly negatively charged</scene> (Glu 156, Glu 160, Glu 183 , Asp 167 et Asp 131 ) and <scene name='Sandbox_Reserved_713/Positively_charged/1'>positively</scene> charged(Lys 132, Lys134, Lys161, His 147, His 151 and Lys 155) | The study of the structure also showed on the surface of the Cu-Binding Site different regions <scene name='Sandbox_Reserved_713/Negatively_charged/1'>highly negatively charged</scene> (Glu 156, Glu 160, Glu 183 , Asp 167 et Asp 131 ) and <scene name='Sandbox_Reserved_713/Positively_charged/1'>positively</scene> charged(Lys 132, Lys134, Lys161, His 147, His 151 and Lys 155) | ||
'''His147''', '''His151''', '''Tyr168''', '''Met170''' are residues that have been identified as able to bind copper. Those four residues are forming a <scene name='Sandbox_Reserved_719/Tetrahedral_coordination_spher/1'>tetrahedral metal binding site</scene> also called tetrahedral coordination sphere. | '''His147''', '''His151''', '''Tyr168''', '''Met170''' are residues that have been identified as able to bind copper. Those four residues are forming a <scene name='Sandbox_Reserved_719/Tetrahedral_coordination_spher/1'>tetrahedral metal binding site</scene> also called tetrahedral coordination sphere. | ||
=== Quaternary structure === | |||
Finally, quaternary structure is formed by two chain A and B, however, there are a few contacts between those two chains. | |||
The strand B0 allows thanks to hydrogen bounds some of those interactions. | |||
There are also some Van der Waals interaction between diffenents aminoacids located on the two chains such as : | |||
His147 (A) and Phe135 (B) | |||
Gly175 (A) and Leu171 (B) | |||
Asp177 (A) and His137 (B) | |||