Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1).
The presence of extensive reciprocal conformational freedom between the catalytic and the hemopexin-like domains of full-length matrix metalloproteinase-1 (MMP-1) is demonstrated by NMR and small angle x-ray scattering experiments. This finding is discussed in relation to the essentiality of the hemopexin-like domain for the collagenolytic activity of MMP-1. The conformational freedom experienced by the present system, having the shortest linker between the two domains, when compared with similar findings on MMP-12 and MMP-9 having longer and the longest linker within the family, respectively, suggests this type of conformational freedom to be a general property of all MMPs.
Bertini
Ivano
I
Magnetic Resonance Center, University of Florence, Sesto Fiorentino, Italy. ivanobertini@cerm.unifi.it
Fragai
Marco
M
Luchinat
Claudio
C
Melikian
Maxime
M
Mylonas
Efstratios
E
Sarti
Niko
N
Svergun
Dmitri I
DI
D002384:Catalysis; D018360:Crystallography, X-Ray; D006418:Heme; D006801:Humans; D020781:Matrix Metalloproteinase 1 / Q000737:chemistry* / Q000378:metabolism*; D053508:Matrix Metalloproteinase 12 / Q000737:chemistry; D020780:Matrix Metalloproteinase 9 / Q000737:chemistry; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D018583:Pliability; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D011994:Recombinant Proteins; D006418:Heme; D020780:Matrix Metalloproteinase 9; D053508:Matrix Metalloproteinase 12; D020781:Matrix Metalloproteinase 1