Substrate Recognition by the Collagen-binding Domain ofClostridium histolyticumClass I Collagenase
作者： Osamu Matsushita , Takaki Koide , Ryoji Kobayashi , Kazuhiro Nagata , Akinobu Okabe
关键词:
摘要: Clostridium histolyticum type I collagenase (ColG) has a segmental structure, S1+S2+S3a+S3b. S3a and S3b bound to insoluble collagen, but S2 did not, thus indicating that S3 forms collagen-binding domain (CBD). Because S3a+S3b showed the most efficient binding substrate, cooperative by both domains was suggested for enzyme. Monomeric (S3b) tandem (S3a+S3b) CBDs atelocollagen, which contains only collagenous region. However, they not bind telopeptides immobilized on Sepharose beads. These results site(s) CBD is(are) present in The peptides, (Pro-Hyp-Gly)(n) (Pro-Pro-Gly)(n), when n is large enough allow peptides have triple-helical conformation. They various with similar amino acid sequences or gelatin, lacks Glc-Gal disaccharide, attached side chains of hydroxylysine residues observations specifically recognizes conformation made three polypeptide
elsevier.com
highwire.org参考文章(30)
Burkhard Rost, PHD: predicting one-dimensional protein structure by profile-based neural networks. Methods in Enzymology. ,vol. 266, pp. 525- 539 ,(1996) , 10.1016/S0076-6879(96)66033-9
T. Tanaka, H. Hidaka, Hydrophobic regions function in calmodulin-enzyme(s) interactions. Journal of Biological Chemistry. ,vol. 255, pp. 11078- 11080 ,(1980) , 10.1016/S0021-9258(19)70253-1
K Yoshihara, O Matsushita, J Minami, A Okabe, Cloning and nucleotide sequence analysis of the colH gene from Clostridium histolyticum encoding a collagenase and a gelatinase. Journal of Bacteriology. ,vol. 176, pp. 6489- 6496 ,(1994) , 10.1128/JB.176.21.6489-6496.1994
O Matsushita, K Yoshihara, S Katayama, J Minami, A Okabe, Purification and characterization of Clostridium perfringens 120-kilodalton collagenase and nucleotide sequence of the corresponding gene. Journal of Bacteriology. ,vol. 176, pp. 149- 156 ,(1994) , 10.1128/JB.176.1.149-156.1994
Magnus Malmqvist, Epitope Mapping by Label-Free Biomolecular Interaction Analysis Methods. ,vol. 9, pp. 525- 532 ,(1996) , 10.1006/METH.1996.0060
Eric G Huizinga, R Martijn van der Plas, Jan Kroon, Jan J Sixma, Piet Gros, Crystal structure of the A3 domain of human von Willebrand factor: implications for collagen binding Structure. ,vol. 5, pp. 1147- 1156 ,(1997) , 10.1016/S0969-2126(97)00266-9
Takaki Koide, Shinichi Asada, Kazuhiro Nagata, SUBSTRATE RECOGNITION OF COLLAGEN-SPECIFIC MOLECULAR CHAPERONE HSP47: STRUCTURAL REQUIREMENTS AND BINDING REGULATION Journal of Biological Chemistry. ,vol. 274, pp. 34523- 34526 ,(1999) , 10.1074/JBC.274.49.34523
J Bella, M Eaton, B Brodsky, H. Berman, Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution. Science. ,vol. 266, pp. 75- 81 ,(1994) , 10.1126/SCIENCE.7695699
Tengiz V. Burjanadze, Hydroxyproline content and location in relation to collagen thermal stability Biopolymers. ,vol. 18, pp. 931- 938 ,(1979) , 10.1002/BIP.1979.360180413
A Nakai, M Satoh, K Hirayoshi, K Nagata, Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum. Journal of Cell Biology. ,vol. 117, pp. 903- 914 ,(1992) , 10.1083/JCB.117.4.903