1u00: Difference between revisions

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[[Image:1u00.jpg|left|200px]]<br /><applet load="1u00" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1u00.jpg|left|200px]]<br /><applet load="1u00" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1u00, resolution 1.95Å" />

'''HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC'''<br />

==Overview==

HscA, a specialized bacterial Hsp70-class molecular chaperone, interacts, with the iron-sulfur cluster assembly protein IscU by recognizing a, conserved LPPVK sequence motif. We report the crystal structure of the, substrate-binding domain of HscA (SBD, residues 389-616) from Escherichia, coli bound to an IscU-derived peptide, ELPPVKIHC. The crystals belong to, the space group I222 and contain a single molecule in the asymmetric unit., Molecular replacement with the E.coli DnaK(SBD) model was used for, phasing, and the HscA(SBD)-peptide model was refined to Rfactor=17.4%, (Rfree=21.0%) at 1.95 A resolution. The overall structure of HscA(SBD) is, similar to that of DnaK(SBD), although the alpha-helical subdomain, (residues 506-613) is shifted up to 10 A relative to the beta-sandwich, subdomain (residues 389-498) when compared to DnaK(SBD). The ELPPVKIHC, peptide is bound in an extended conformation in a hydrophobic cleft in the, beta-subdomain, which appears to be solvent-accessible via a narrow, passageway between the alpha and beta-subdomains. The bound peptide is, positioned in the reverse orientation of that observed in the, DnaK(SBD)-NRLLLTG peptide complex placing the N and C termini of the, peptide on opposite sides of the HscA(SBD) relative to the DnaK(SBD), complex. Modeling of the peptide in the DnaK-like forward orientation, suggests that differences in hydrogen bonding interactions in the binding, cleft and electrostatic interactions involving surface residues near the, cleft contribute to the observed directional preference.

HscA, a specialized bacterial Hsp70-class molecular chaperone, interacts with the iron-sulfur cluster assembly protein IscU by recognizing a conserved LPPVK sequence motif. We report the crystal structure of the substrate-binding domain of HscA (SBD, residues 389-616) from Escherichia coli bound to an IscU-derived peptide, ELPPVKIHC. The crystals belong to the space group I222 and contain a single molecule in the asymmetric unit. Molecular replacement with the E.coli DnaK(SBD) model was used for phasing, and the HscA(SBD)-peptide model was refined to Rfactor=17.4% (Rfree=21.0%) at 1.95 A resolution. The overall structure of HscA(SBD) is similar to that of DnaK(SBD), although the alpha-helical subdomain (residues 506-613) is shifted up to 10 A relative to the beta-sandwich subdomain (residues 389-498) when compared to DnaK(SBD). The ELPPVKIHC peptide is bound in an extended conformation in a hydrophobic cleft in the beta-subdomain, which appears to be solvent-accessible via a narrow passageway between the alpha and beta-subdomains. The bound peptide is positioned in the reverse orientation of that observed in the DnaK(SBD)-NRLLLTG peptide complex placing the N and C termini of the peptide on opposite sides of the HscA(SBD) relative to the DnaK(SBD) complex. Modeling of the peptide in the DnaK-like forward orientation suggests that differences in hydrogen bonding interactions in the binding cleft and electrostatic interactions involving surface residues near the cleft contribute to the observed directional preference.

==About this Structure==

1U00 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1U00 OCA].

1U00 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U00 OCA].

==Reference==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Cupp-Vickery, J.R.]]

[[Category: Cupp-Vickery, J R.]]

[[Category: Peterson, J.C.]]

[[Category: Peterson, J C.]]

[[Category: Ta, D.T.]]

[[Category: Ta, D T.]]

[[Category: Vickery, L.E.]]

[[Category: Vickery, L E.]]

[[Category: dnak]]

[[Category: hsc66]]

Line 23:

[[Category: iscu]]

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@@ Line 1: / Line 1: @@
-[[Image:1u00.jpg|left|200px]]<br /><applet load="1u00" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1u00.jpg|left|200px]]<br /><applet load="1u00" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1u00, resolution 1.95&Aring;" />
 '''HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC'''<br />
 ==Overview==
-HscA, a specialized bacterial Hsp70-class molecular chaperone, interacts, with the iron-sulfur cluster assembly protein IscU by recognizing a, conserved LPPVK sequence motif. We report the crystal structure of the, substrate-binding domain of HscA (SBD, residues 389-616) from Escherichia, coli bound to an IscU-derived peptide, ELPPVKIHC. The crystals belong to, the space group I222 and contain a single molecule in the asymmetric unit., Molecular replacement with the E.coli DnaK(SBD) model was used for, phasing, and the HscA(SBD)-peptide model was refined to Rfactor=17.4%, (Rfree=21.0%) at 1.95 A resolution. The overall structure of HscA(SBD) is, similar to that of DnaK(SBD), although the alpha-helical subdomain, (residues 506-613) is shifted up to 10 A relative to the beta-sandwich, subdomain (residues 389-498) when compared to DnaK(SBD). The ELPPVKIHC, peptide is bound in an extended conformation in a hydrophobic cleft in the, beta-subdomain, which appears to be solvent-accessible via a narrow, passageway between the alpha and beta-subdomains. The bound peptide is, positioned in the reverse orientation of that observed in the, DnaK(SBD)-NRLLLTG peptide complex placing the N and C termini of the, peptide on opposite sides of the HscA(SBD) relative to the DnaK(SBD), complex. Modeling of the peptide in the DnaK-like forward orientation, suggests that differences in hydrogen bonding interactions in the binding, cleft and electrostatic interactions involving surface residues near the, cleft contribute to the observed directional preference.
+HscA, a specialized bacterial Hsp70-class molecular chaperone, interacts with the iron-sulfur cluster assembly protein IscU by recognizing a conserved LPPVK sequence motif. We report the crystal structure of the substrate-binding domain of HscA (SBD, residues 389-616) from Escherichia coli bound to an IscU-derived peptide, ELPPVKIHC. The crystals belong to the space group I222 and contain a single molecule in the asymmetric unit. Molecular replacement with the E.coli DnaK(SBD) model was used for phasing, and the HscA(SBD)-peptide model was refined to Rfactor=17.4% (Rfree=21.0%) at 1.95 A resolution. The overall structure of HscA(SBD) is similar to that of DnaK(SBD), although the alpha-helical subdomain (residues 506-613) is shifted up to 10 A relative to the beta-sandwich subdomain (residues 389-498) when compared to DnaK(SBD). The ELPPVKIHC peptide is bound in an extended conformation in a hydrophobic cleft in the beta-subdomain, which appears to be solvent-accessible via a narrow passageway between the alpha and beta-subdomains. The bound peptide is positioned in the reverse orientation of that observed in the DnaK(SBD)-NRLLLTG peptide complex placing the N and C termini of the peptide on opposite sides of the HscA(SBD) relative to the DnaK(SBD) complex. Modeling of the peptide in the DnaK-like forward orientation suggests that differences in hydrogen bonding interactions in the binding cleft and electrostatic interactions involving surface residues near the cleft contribute to the observed directional preference.
 ==About this Structure==
-U00 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U00 OCA].
+U00 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U00 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Cupp-Vickery, J.R.]]
+[[Category: Cupp-Vickery, J R.]]
-[[Category: Peterson, J.C.]]
+[[Category: Peterson, J C.]]
-[[Category: Ta, D.T.]]
+[[Category: Ta, D T.]]
-[[Category: Vickery, L.E.]]
+[[Category: Vickery, L E.]]
 [[Category: dnak]]
 [[Category: hsc66]]
@@ Line 23: / Line 23: @@
 [[Category: iscu]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:44:18 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:09 2008''