Structures of three polycystic kidney disease-like domains from Clostridium histolyticum collagenases ColG and ColH

Acta Crystallographica. Section D, Biological Crystallography
Ryan BauerJoshua Sakon

Abstract

Clostridium histolyticum collagenases ColG and ColH are segmental enzymes that are thought to be activated by Ca(2+)-triggered domain reorientation to cause extensive tissue destruction. The collagenases consist of a collagenase module (s1), a variable number of polycystic kidney disease-like (PKD-like) domains (s2a and s2b in ColH and s2 in ColG) and a variable number of collagen-binding domains (s3 in ColH and s3a and s3b in ColG). The X-ray crystal structures of Ca(2+)-bound holo s2b (1.4 Å resolution, R = 15.0%, Rfree = 19.1%) and holo s2a (1.9 Å resolution, R = 16.3%, Rfree = 20.7%), as well as of Ca(2+)-free apo s2a (1.8 Å resolution, R = 20.7%, Rfree = 27.2%) and two new forms of N-terminally truncated apo s2 (1.4 Å resolution, R = 16.9%, Rfree = 21.2%; 1.6 Å resolution, R = 16.2%, Rfree = 19.2%), are reported. The structurally similar PKD-like domains resemble the V-set Ig fold. In addition to a conserved β-bulge, the PKD-like domains feature a second bulge that also changes the allegiance of the subsequent β-strand. This β-bulge and the genesis of a Ca(2+) pocket in the archaeal PKD-like domain suggest a close kinship between bacterial and archaeal PKD-like domains. Different surface properties and indications of diffe...Continue Reading

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Citations

May 20, 2016·Journal of Diabetes Research·Hiroki ShimaKazutaka Murayama
Jul 8, 2015·Applied and Environmental Microbiology·Yu-Zhong ZhangXiu-Lan Chen
Feb 20, 2021·Scientific Reports·Isabel J HoppeEsther Schönauer

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Methods Mentioned

BETA
NMR
X-ray
fluorescence spectroscopy
surface plasmon resonance

Software Mentioned

REFMAC
MolProbity
PARVATI
3000
Phaser
Anisotropic Network Model ( ANM )
MIFit
TREK
CASTp

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