2HLC

HL COLLAGENASE STRUCTURE AT 1.7A RESOLUTION

Summary for 2HLC

• Entry DOI: 10.2210/pdb2hlc/pdb
• Descriptor: COLLAGENASE (2 entities in total)
• Functional Keywords: serine protease, hydrolase, collagen degradation
• Biological source: Hypoderma lineatum (early cattle grub)
• Cellular location: Secreted: P08897
• Total number of polymer chains: 2
• Total formula weight: 50494.38

Authors

Broutin, I.,Merigeau, K.,Arnoux, B.,Ducruix, A. (deposition date: 1997-01-08, release date: 1997-09-04, Last modification date: 2025-11-12)

Primary citation

Broutin-L'Hermite, I.,Ries-Kautt, M.,Ducruix, A.
1.7 A x-ray structure of space-grown collagenase crystals.
Acta Crystallogr.,Sect.D, 56:376-378, 2000

PubMed Abstract: Collagenases, divided into metallocollagenases and serine collagenases, are the only proteases that cleave the triple helix of collagen under physiological conditions. In the present work, the serine protease collagenase purified from Hypoderma lineatum larvae is studied. From crystals grown in the International Microgravity Laboratory (IML2), a data set was collected at 1.7 A using synchrotron radiation. Although the resolution is not very different, the signal-to-noise ratio and the quality of the electron density are much improved. Alternate conformations were revealed for several residues, in particular Tyr99, suggesting a gate mechanism of recognition.

PubMed: 10713532
DOI: 10.1107/s0907444999016789

Experimental method

X-RAY DIFFRACTION (1.7 Å)