Bacterial collagen-like proteins that form triple-helical structures.
Bacterial collagen-like proteins that form triple-helical structures.
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DOI:
10.1016/j.jsb.2014.01.003
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发表时间:
2014-06
影响因子:
3
通讯作者:
Brodsky, Barbara
中科院分区:
文献类型:
--
作者:
Yu, Zhuoxin;An, Bo;Ramshaw, John A. M.;Brodsky, Barbara
A large number of collagen-like proteins have been identified in bacteria during the past ten years, principally from analysis of genome databases. These bacterial collagens share the distinctive Gly-Xaa-Yaa repeating amino acid sequence of animal collagens which underlies their unique triple-helical structure. A number of the bacterial collagens have been expressed in E. coli, and they all adopt a triple-helix conformation. Unlike animal collagens, these bacterial proteins do not contain the post-translationally modified amino acid, hydroxyproline, which is known to stabilize the triple-helix structure and may promote self-assembly. Despite the absence of collagen hydroxylation, the triple-helix structures of the bacterial collagens studied exhibit a high thermal stability of 35–39 °C, close to that seen for mammalian collagens. These bacterial collagens are readily produced in large quantities by recombinant methods, either in the original amino acid sequence or in genetically manipulated sequences. This new family of recombinant, easy to modify collagens could provide a novel system for investigating structural and functional motifs in animal collagens and could also form the basis of new biomedical materials with designed structural properties and functions.
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影响因子:
2.9
作者:
Culpepper, Megen A.;Scott, Emily E.;Limburg, Julian
通讯作者:
Limburg, Julian
影响因子:
4.8
作者:
Daubenspeck, JM;Zeng, HD;Turnbough, CL
通讯作者:
Turnbough, CL
影响因子:
56.9
作者:
BELLA, J;EATON, M;BERMAN, HM
通讯作者:
BERMAN, HM
DOI:
10.4161/bbug.1.2.10484
发表时间:
2010-03-01
期刊:
Bioengineered bugs
影响因子:
--
作者:
Adrio, Jose-Luis;Demain, Arnold L
通讯作者:
Demain, Arnold L
影响因子:
6.2
作者:
Browning, Mary Beth;Russell, Brooke;Cosgriff-Hernandez, Elizabeth M.
通讯作者:
Cosgriff-Hernandez, Elizabeth M.