1u00
From Proteopedia
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'''HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC''' | '''HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC''' | ||
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[[Category: Ta, D T.]] | [[Category: Ta, D T.]] | ||
[[Category: Vickery, L E.]] | [[Category: Vickery, L E.]] | ||
| - | [[Category: | + | [[Category: Dnak]] |
| - | [[Category: | + | [[Category: Hsc66]] |
| - | [[Category: | + | [[Category: Hsca]] |
| - | [[Category: | + | [[Category: Hsp70]] |
| - | [[Category: | + | [[Category: Iscu]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:34:36 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:34, 3 May 2008
HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC
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.
About this Structure
1U00 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC., Cupp-Vickery JR, Peterson JC, Ta DT, Vickery LE, J Mol Biol. 2004 Sep 24;342(4):1265-78. PMID:15351650 Page seeded by OCA on Sat May 3 10:34:36 2008
Categories: Escherichia coli | Single protein | Cupp-Vickery, J R. | Peterson, J C. | Ta, D T. | Vickery, L E. | Dnak | Hsc66 | Hsca | Hsp70 | Iscu
