Structural Comparison of ColH and ColG Collagen-Binding Domains from Clostridium histolyticum

Bauer, Ryan; Wilson, Jeffrey J.; Philominathan, Sagaya Theresa Leena; Davis, Danny J.; Matsushita, Osamu; Sakon, J.

doi:10.1128/jb.00010-12

Cited by 31 publications

(46 citation statements)

References 45 publications

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“…Although the overall structure of Clostridium collagenases is still not completely known, the crystal structures of the collagenase unit of ColG (20), the peptidase domains of ColH and ColT (21), the PKD-like domains of ColG and ColH (22,23), and the CBDs of ColG and ColH (24,25) have been solved. The N-terminal activator domain and the C-terminal peptidase domain in the collagenase unit of ColG form a saddle-shaped architecture.…”

Section: Structurementioning

confidence: 99%

“…The CBDs from ColG and ColH adopt a ␤-sheet sandwich fold, in which a collagen-binding cleft is seen. Two calcium ions are coordinated in a CBD molecule, and these are critical for maintaining the function and stability of the CBDs (24,25). It has not yet been determined whether the CBD can function as a helicase to unwind the collagen triple helix.…”

Section: Structurementioning

confidence: 99%

“…The (20) are colored in purple and gray, respectively, and the PKD (PDB accession number 4AQO) (21) and the CBD (PDB accession number 1NQD) (24) are colored in yellow and orange, respectively. For ColH, the peptidase domain (PDB accession number 4AR1) (21), the PKD (PDB accession number 4U7K) (23), and the CBD (PDB accession number 3JQW) (25) are colored in gray, yellow, and orange, respectively. The catalytic domains of both MCP-01 (PDB accession number 3VV3) (65) and kumamolisin-As (PDB accession number 1SN7) (72) are shown in gray.…”

Section: Bacterial Serine Collagenolytic Proteases From the S1 Familymentioning

confidence: 99%

See 2 more Smart Citations

Diversity, Structures, and Collagen-Degrading Mechanisms of Bacterial Collagenolytic Proteases

Zhang¹,

Ran²,

Li³

et al. 2015

Appl Environ Microbiol

108

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Bacterial collagenolytic proteases are important because of their essential role in global collagen degradation and because of their virulence in some human bacterial infections. Bacterial collagenolytic proteases include some metalloproteases of the M9 family from Clostridium or Vibrio strains, some serine proteases distributed in the S1, S8, and S53 families, and members of the U32 family. In recent years, there has been remarkable progress in discovering new bacterial collagenolytic proteases and in investigating the collagen-degrading mechanisms of bacterial collagenolytic proteases. This review provides comprehensive insight into bacterial collagenolytic proteases, especially focusing on the structures and collagen-degrading mechanisms of representative bacterial collagenolytic proteases in each family. The roles of bacterial collagenolytic proteases in human diseases and global nitrogen cycling, together with the biotechnological and medical applications for these proteases, are also briefly discussed.

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Section: Structurementioning

confidence: 99%

Section: Structurementioning

confidence: 99%

Section: Bacterial Serine Collagenolytic Proteases From the S1 Familymentioning

confidence: 99%

See 1 more Smart Citation

Diversity, Structures, and Collagen-Degrading Mechanisms of Bacterial Collagenolytic Proteases

Zhang¹,

Ran²,

Li³

et al. 2015

Appl Environ Microbiol

108

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“…; Bauer et al . ). Other research showed that the collagen‐binding segment was not necessary to degrade gelatin (denatured, nontriple‐helical collagen) and acid‐solubilized collagen (Philominathan et al .…”

Section: C‐terminal Protease Domains Are Involved In Protein–protein mentioning

confidence: 97%

C-terminal domains of bacterial proteases: structure, function and the biotechnological applications

Huang

Liú

et al. 2016

J Appl Microbiol

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Summary C‐terminal domains widely exist in the C‐terminal region of multidomain proteases. As a β‐sandwich domain in multidomain protease, the C‐terminal domain plays an important role in proteolysis including regulation of the secretory process, anchoring and swelling the substrate molecule, presenting as an inhibitor for the preprotease and adapting the protein structural flexibility and stability. In this review, the diversity, structural characteristics and biological function of C‐terminal protease domains are described. Furthermore, the application prospects of C‐terminal domains, including polycystic kidney disease, prepeptidase C‐terminal and collagen‐binding domain, in the area of medicine and biological artificial materials are also discussed.

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“…Clostridium histolyticum class II collagenase (ColH) contains two polycystic kidney disease (PKD) domains and one collagenbinding domain (CBD), which are necessary for the catalytic activity and collagen-binding affinity of this enzyme. 29,30 We previously fused the CBD and PKD domain of ColH to bFGF and demonstrated that the resulting bFGF-PKD-CBD fusion protein had higher in-vitro collagen-binding ability compared to bFGF-CBD and enhanced bone formation compared to native bFGF and bFGF-CBD when grafted together with collagen in a rat femur. 31,32 In addition, the combination of injectable collagen powder and bFGF-PKD-CBD markedly accelerated bone formation in a mouse femur fracture model compared to treatment with bFGF alone.…”

Section: Introductionmentioning

confidence: 99%

Acceleration of bone formation during fracture healing by poly(pro–hyp–gly)₁₀ and basic fibroblast growth factor containing polycystic kidney disease and collagen‐binding domains from Clostridium histolyticum collagenase

Sekiguchi

Uchida

Inoue

et al. 2016

J Biomedical Materials Res

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Growth factor delivered in combination with animal-derived collagen materials has been used to accelerate bone fracture healing in human patients. However, the introduction of bovine proteins into humans carries the risk of zoonotic and immunologic complications. Here, we developed a collagen-like polypeptide-based bone formation system consisting of poly(Pro-Hyp-Gly)10 , which mimics the triple helical conformation of collagen, and basic fibroblast growth factor (bFGF) fused to the polycystic kidney disease (PKD) domain and collagen-binding domain (CBD) of Clostridium histolyticum collagenase. Circular dichroism spectral analysis showed that when pepsin-soluble bovine type I collagen was treated at 50°C, a positive signal corresponding to the collagen triple helix at 220 nm was not detected. In contrast, poly(Pro-Hyp-Gly)10 retained the 220-nm positive peak, even when treated at 80°C. The combination of the collagen binding-bFGF fusion protein (bFGF-PKD-CBD) with poly(Pro-Hyp-Gly)10 induced greater bone formation compared to bFGF alone in mice bone fracture models. Taken together, these properties suggest that the bFGF-PKD-CBD/poly(Pro-Hyp-Gly)10 composite is a promising material for bone repair in the clinical setting. © 2016 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 104A: 1372-1378, 2016.

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Structural Comparison of ColH and ColG Collagen-Binding Domains from Clostridium histolyticum

Cited by 31 publications

References 45 publications

Diversity, Structures, and Collagen-Degrading Mechanisms of Bacterial Collagenolytic Proteases

Diversity, Structures, and Collagen-Degrading Mechanisms of Bacterial Collagenolytic Proteases

C-terminal domains of bacterial proteases: structure, function and the biotechnological applications

Acceleration of bone formation during fracture healing by poly(pro–hyp–gly)₁₀ and basic fibroblast growth factor containing polycystic kidney disease and collagen‐binding domains from Clostridium histolyticum collagenase

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Structural Comparison of ColH and ColG Collagen-Binding Domains from Clostridium histolyticum

Cited by 31 publications

References 45 publications

Diversity, Structures, and Collagen-Degrading Mechanisms of Bacterial Collagenolytic Proteases

Diversity, Structures, and Collagen-Degrading Mechanisms of Bacterial Collagenolytic Proteases

C-terminal domains of bacterial proteases: structure, function and the biotechnological applications

Acceleration of bone formation during fracture healing by poly(pro–hyp–gly)10 and basic fibroblast growth factor containing polycystic kidney disease and collagen‐binding domains from Clostridium histolyticum collagenase

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Acceleration of bone formation during fracture healing by poly(pro–hyp–gly)₁₀ and basic fibroblast growth factor containing polycystic kidney disease and collagen‐binding domains from Clostridium histolyticum collagenase