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Sub-Ångstrom structure of collagen model peptide (GPO)10 shows a hydrated triple helix with pitch variation and two proline ring conformations.

Abstract：

:Collagens are large structural proteins that are prevalent in mammalian connective tissue. Peptides designed to include a glycine-proline-hydroxyproline (GPO) amino acid triad are biomimetic analogs of the collagen triple helix, a fold that is a hallmark of collagen-like sequences. To inform the rational engineering of collagen-like peptides and proteins for food systems, we report the crystal structure of the (GPO)10 peptide at 0.89-Å resolution, solved using direct methods. We determined that a single chain in the asymmetric unit forms a pseudo-hexagonal network of triple helices that have a pitch variation consistent with the model 7/2 helix (3.5 residues per turn). The proline rings occupied one of two states, while the helix was found to have a well-defined hydration shell involved in the stabilization of the inter-helix crystal network. This structure offers a new high-resolution basis for understanding the hierarchical assembly of native collagens, which will aid the food industry in engineering new sustainable food systems.

journal_name

Food Chem

journal_title

Food chemistry

authors

Suzuki H,Mahapatra D,Board AJ,Steel PJ,Dyer JM,Gerrard JA,Dobson RCJ,Valéry C

doi

10.1016/j.foodchem.2020.126598

subject

Has Abstract

pub_date

2020-07-30 00:00:00

pages

126598

eissn

0308-8146

issn

1873-7072

pii

S0308-8146(20)30460-X

journal_volume

319

pub_type

杂志文章

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