1ofi

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Revision as of 17:48, 29 October 2007

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spinqualitylabelsall models 1ofi, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

ASYMMETRIC COMPLEX BETWEEN HSLV AND I-DOMAIN DELETED HSLU (H. INFLUENZAE)

Overview

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 Structure

1OFI is a [Protein complex] structure of sequences from [Haemophilus influenzae] with PO4, MG, ADP and LVS as [ligands]. Full crystallographic information is available from [OCA].

Reference

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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