The structures of HsIU and the ATP-dependent protease HsIU-HsIV
Article Abstract:
It has been possible to identify the crystal structures of free Hs1U, a member of the Hsp100 family of ATPases, and an 820,000 relative molecular mass complex of Hs1U and Hs1V. This is the first structure of an entire set of components of an ATP-dependent protease. This research involved expressing and purifying histidine-tagged variants of Hs1V and Hs1U from Escherichia coli. It is suggested that the proteasomal ATPases are structurally similar to Hs1U but have the I domain fused to the N terminus, which is close.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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Structure of 20S proteasome from yeast at 2.4A resolution
Article Abstract:
The yeast Sacchararomyces cerevisiae's 20S proteasome has a similar size and structure as the archaebacterial proteasome but a greater complexity. It comprises 28 protein subunits arranged as four homoheptameric rings. The particle's interior, which contains the active sites, is accessible only by narrow side windows. The crystallographic structural analysis of the yeast 20S proteasome is described.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Structure of cytochrome c nitrite reductase
Article Abstract:
The crystal structure of the cytochrome C nitrite reductase enzyme from the microorganism Sulfurospirillum deleyianum is reported. A reaction scheme is proposed to transform the nitrite based on structural and spectroscopic data. The haem arrangement is compared with that of other multi-haem cytochromes, and a family of proteins where the orientation of haem groups is conserved, while structure and function are not, has been identified.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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