2Y6I

Crystal Structure of Collagenase G from Clostridium histolyticum in complex with Isoamylphosphonyl-Gly-Pro-Ala at 3.25 Angstrom Resolution

Summary for 2Y6I

• Entry DOI: 10.2210/pdb2y6i/pdb
• Related: 2Y3U 2Y50
• Related PRD ID: PRD_000989
• Descriptor: COLLAGENASE, ISOAMYLPHOSPHONYL-GLY-PRO-ALA, ZINC ION, ... (8 entities in total)
• Functional Keywords: hydrolase-inhibitor complex, hydrolase, gluzincin, metalloprotease, hydrolase/inhibitor
• Biological source: CLOSTRIDIUM HISTOLYTICUM; More
• Total number of polymer chains: 2
• Total formula weight: 90480.77

Authors

Eckhard, U.,Brandstetter, H. (deposition date: 2011-01-21, release date: 2011-09-28, Last modification date: 2024-10-09)

Primary citation

Eckhard, U.,Schoenauer, E.,Nuess, D.,Brandstetter, H.
Structure of Collagenase G Reveals a Chew-and -Digest Mechanism of Bacterial Collagenolysis
Nat.Struct.Mol.Biol., 18:1109-, 2011

PubMed Abstract: Collagen constitutes one-third of body protein in humans, reflecting its extensive role in health and disease. Of similar importance, therefore, are the idiosyncratic proteases that have evolved for collagen remodeling. The most efficient collagenases are those that enable clostridial bacteria to colonize their host tissues; but despite intense study, the structural and mechanistic basis of these enzymes has remained elusive. Here we present the crystal structure of collagenase G from Clostridium histolyticum at 2.55-Å resolution. By combining the structural data with enzymatic and mutagenesis studies, we derive a conformational two-state model of bacterial collagenolysis, in which recognition and unraveling of collagen microfibrils into triple helices, as well as unwinding of the triple helices, are driven by collagenase opening and closing.

PubMed: 21947205
DOI: 10.1038/NSMB.2127

Experimental method

X-RAY DIFFRACTION (3.25 Å)