1ofh
ASYMMETRIC COMPLEX BETWEEN HSLV AND I-DOMAIN DELETED HSLU (H. INFLUENZAE)
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OverviewOverview
In the prokaryotic homolog of the eukaryotic proteasome, HslUV, the, "double donut" HslV protease is allosterically activated by HslU, an AAA, protein of the Clp/Hsp100 family consisting of three (amino-terminal, carboxy-terminal, and intermediate) domains. The intermediate domains of, HslU, which extend like tentacles from the hexameric ring formed by the, amino-terminal and carboxy-terminal domains, have been deleted; an, asymmetric HslU(DeltaI)(6)HslV(12) complex has been crystallized; and the, structure has been solved to 2.5A resolution, revealing an assembly in, which a HslU(DeltaI) hexamer binds one end of the HslV dodecamer. The, conformation of the protomers of the HslU(DeltaI)-complexed HslV hexamer, is similar to that in the symmetric wild-type HslUV complex, while the, ... [(full description)]
About this StructureAbout this Structure
1OFH is a [Protein complex] structure of sequences from [Haemophilus influenzae] with PO4, MG and ADP as [ligands]. Full crystallographic information is available from [OCA].
ReferenceReference
Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome., Kwon AR, Kessler BM, Overkleeft HS, McKay DB, J Mol Biol. 2003 Jul 4;330(2):185-95. PMID:12823960
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