1slf: Difference between revisions

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[[Image:1slf.gif|left|200px]]<br /><applet load="1slf" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1slf.gif|left|200px]]<br /><applet load="1slf" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1slf, resolution 1.76Å" />

'''APOSTREPTAVIDIN, PH 5.6, TWO MOLECULES OF (SO4)2 BOUND AT THE BIOTIN BINDING SITE'''<br />

==Overview==

The streptavidin-bound crystal structures of two disulfide-bridge cyclic, peptides (cyclo-Ac-[CHPQGPPC]-NH2 and cyclo-Ac-[CHPQFC]-NH2) and of a, linear peptide (FSHPQNT) were determined, as well as the structure of, apostreptavidin (streptavidin-sulfate). Both the linear and, disulfide-bridged cyclic peptides studied share a common HPQ conformation, and make common interactions with streptavidin, although significant, differences in structures and interactions occur for flanking residues, among the complexes. The conformation of the linear peptide in the crystal, structure of streptavidin-FSHPQNT was found to differ from that in the, same complex published [Weber, P. C., Pantoliano, M. W., & Thompson, L. D., (1992) Biochemistry 31, 9350-9354]. In the present investigation, the, HPQNT portion of the ligand is well-defined with some density defining the, Phe, whereas in the investigation of Weber et al. only the HPQ segment of, the bound peptide could be interpreted. Both bound cyclic peptides adopt a, beta-turn involving an H-bond between the His main chain carbonyl and the, main chain amide NH of the i+3 residue. In the streptavidin-bound, cyclo-Ac-[CHPQFC]-NH2 structure, there is an additional H-bond, indicative, of alpha-helix, between the main chain His carbonyl and the main chain, C-terminal Cys amide NH group. Binding interactions for both cyclic and, linear peptides include direct H-bonds, H-bonds mediated by tightly bound, water molecules, and hydrophobic interactions. The above structures and, that of streptavidin-biotin in the literature are compared and discussed, in the context of structure-based ligand design.

The streptavidin-bound crystal structures of two disulfide-bridge cyclic peptides (cyclo-Ac-[CHPQGPPC]-NH2 and cyclo-Ac-[CHPQFC]-NH2) and of a linear peptide (FSHPQNT) were determined, as well as the structure of apostreptavidin (streptavidin-sulfate). Both the linear and disulfide-bridged cyclic peptides studied share a common HPQ conformation and make common interactions with streptavidin, although significant differences in structures and interactions occur for flanking residues among the complexes. The conformation of the linear peptide in the crystal structure of streptavidin-FSHPQNT was found to differ from that in the same complex published [Weber, P. C., Pantoliano, M. W., & Thompson, L. D. (1992) Biochemistry 31, 9350-9354]. In the present investigation, the HPQNT portion of the ligand is well-defined with some density defining the Phe, whereas in the investigation of Weber et al. only the HPQ segment of the bound peptide could be interpreted. Both bound cyclic peptides adopt a beta-turn involving an H-bond between the His main chain carbonyl and the main chain amide NH of the i+3 residue. In the streptavidin-bound cyclo-Ac-[CHPQFC]-NH2 structure, there is an additional H-bond, indicative of alpha-helix, between the main chain His carbonyl and the main chain C-terminal Cys amide NH group. Binding interactions for both cyclic and linear peptides include direct H-bonds, H-bonds mediated by tightly bound water molecules, and hydrophobic interactions. The above structures and that of streptavidin-biotin in the literature are compared and discussed in the context of structure-based ligand design.

==About this Structure==

1SLF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1SLF OCA].

1SLF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLF OCA].

==Reference==

Line 13:

[[Category: Single protein]]

[[Category: Streptomyces avidinii]]

[[Category: Katz, B.A.]]

[[Category: Katz, B A.]]

[[Category: SO4]]

[[Category: biotin-binding protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 02:~~27:44 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:46 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1slf.gif|left|200px]]<br /><applet load="1slf" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1slf.gif|left|200px]]<br /><applet load="1slf" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1slf, resolution 1.76&Aring;" />
 '''APOSTREPTAVIDIN, PH 5.6, TWO MOLECULES OF (SO4)2 BOUND AT THE BIOTIN BINDING SITE'''<br />
 ==Overview==
-The streptavidin-bound crystal structures of two disulfide-bridge cyclic, peptides (cyclo-Ac-[CHPQGPPC]-NH2 and cyclo-Ac-[CHPQFC]-NH2) and of a, linear peptide (FSHPQNT) were determined, as well as the structure of, apostreptavidin (streptavidin-sulfate). Both the linear and, disulfide-bridged cyclic peptides studied share a common HPQ conformation, and make common interactions with streptavidin, although significant, differences in structures and interactions occur for flanking residues, among the complexes. The conformation of the linear peptide in the crystal, structure of streptavidin-FSHPQNT was found to differ from that in the, same complex published [Weber, P. C., Pantoliano, M. W., &amp; Thompson, L. D., (1992) Biochemistry 31, 9350-9354]. In the present investigation, the, HPQNT portion of the ligand is well-defined with some density defining the, Phe, whereas in the investigation of Weber et al. only the HPQ segment of, the bound peptide could be interpreted. Both bound cyclic peptides adopt a, beta-turn involving an H-bond between the His main chain carbonyl and the, main chain amide NH of the i+3 residue. In the streptavidin-bound, cyclo-Ac-[CHPQFC]-NH2 structure, there is an additional H-bond, indicative, of alpha-helix, between the main chain His carbonyl and the main chain, C-terminal Cys amide NH group. Binding interactions for both cyclic and, linear peptides include direct H-bonds, H-bonds mediated by tightly bound, water molecules, and hydrophobic interactions. The above structures and, that of streptavidin-biotin in the literature are compared and discussed, in the context of structure-based ligand design.
+The streptavidin-bound crystal structures of two disulfide-bridge cyclic peptides (cyclo-Ac-[CHPQGPPC]-NH2 and cyclo-Ac-[CHPQFC]-NH2) and of a linear peptide (FSHPQNT) were determined, as well as the structure of apostreptavidin (streptavidin-sulfate). Both the linear and disulfide-bridged cyclic peptides studied share a common HPQ conformation and make common interactions with streptavidin, although significant differences in structures and interactions occur for flanking residues among the complexes. The conformation of the linear peptide in the crystal structure of streptavidin-FSHPQNT was found to differ from that in the same complex published [Weber, P. C., Pantoliano, M. W., &amp; Thompson, L. D. (1992) Biochemistry 31, 9350-9354]. In the present investigation, the HPQNT portion of the ligand is well-defined with some density defining the Phe, whereas in the investigation of Weber et al. only the HPQ segment of the bound peptide could be interpreted. Both bound cyclic peptides adopt a beta-turn involving an H-bond between the His main chain carbonyl and the main chain amide NH of the i+3 residue. In the streptavidin-bound cyclo-Ac-[CHPQFC]-NH2 structure, there is an additional H-bond, indicative of alpha-helix, between the main chain His carbonyl and the main chain C-terminal Cys amide NH group. Binding interactions for both cyclic and linear peptides include direct H-bonds, H-bonds mediated by tightly bound water molecules, and hydrophobic interactions. The above structures and that of streptavidin-biotin in the literature are compared and discussed in the context of structure-based ligand design.
 ==About this Structure==
-SLF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SLF OCA].
+SLF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLF OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Streptomyces avidinii]]
-[[Category: Katz, B.A.]]
+[[Category: Katz, B A.]]
 [[Category: SO4]]
 [[Category: biotin-binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:27:44 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:46 2008''