PDBsum entry 1sop

Structural protein

PDB id: 1sop

Contents

Protein chain

26 a.a.

PDB id:

1sop

Name:

Structural protein

Title:

C-terminal cystine-rich domain of minicollagen-i from hydra

Structure:

Mini-collagen. Chain: a. Fragment: c-terminal cystine-rich domain. Engineered: yes

Source:

Synthetic: yes. Other_details: fmoc solid phase synthesis + oxidation. The sequence is naturally found in hydra sp.

NMR struc:

10 models

Authors:

A.G.Milbradt,L.Moroder,C.Renner

Key ref:

E.Pokidysheva et al. (2004). The structure of the Cys-rich terminal domain of Hydra minicollagen, which is involved in disulfide networks of the nematocyst wall. J Biol Chem, 279, 30395-30401. PubMed id: 15123641 DOI: 10.1074/jbc.M403734200

Date:

15-Mar-04 Release date: 27-Apr-04

Protein chain

Q00484  (Q00484_9CNID) -  Mini-collagen from Hydra sp

Seq: 149 a.a.

Struc: 25 a.a.

DOI no: 10.1074/jbc.M403734200

J Biol Chem 279:30395-30401 (2004)

PubMed id: 15123641

The structure of the Cys-rich terminal domain of Hydra minicollagen, which is involved in disulfide networks of the nematocyst wall.

E.Pokidysheva, A.G.Milbradt, S.Meier, C.Renner, D.Häussinger, H.P.Bächinger, L.Moroder, S.Grzesiek, T.W.Holstein, S.Ozbek, J.Engel.

ABSTRACT

The minicollagens found in the nematocysts of Hydra constitute a family of invertebrate collagens with unusual properties. They share a common modular architecture with a central collagen sequence ranging from 14 to 16 Gly-X-Y repeats flanked by polyproline/hydroxyproline stretches and short terminal domains that show a conserved cysteine pattern (CXXXCXXXCXXX-CXXXCC). The minicollagen cysteine-rich domains are believed to function in a switch of the disulfide connectivity from intra- to intermolecular bonds during maturation of the capsule wall. The solution structure of the C-terminal fragment including a minicollagen cysteine-rich domain of minicollagen-1 was determined in two independent groups by 1H NMR. The corresponding peptide comprising the last 24 residues of the molecule was produced synthetically and refolded by oxidation under low protein concentrations. Both presented structures are identical in their fold and disulfide connections (Cys2-Cys18, Cys6-Cys14, and Cys10-Cys19) revealing a robust structural motif that is supposed to serve as the polymerization module of the nematocyst capsule.

Selected figure(s)

Figure 1.
FIG. 1. A, minicollagen-1 amino acid sequence and domain structure. The propeptide sequence is blue, the MCRDs are red, polyproline sequences are light green, the collagen repeat is dark green. B, alignment of MCRDs in minicollagen molecules from different cnidarians and in NOWA. MCol1h, minicollagen-1 Hydra; MCol2h, minicollagen-2 Hydra (3); MColad, minicollagen Acropora donei (2); MColac, minicollagen Acropora cervicornis (1); MColap, minicollagen Acropora palmate (1); N and C, N-, C-terminal. The sequence of the Cys-rich region of NOWA in Hydra (NWh) starts with repeat 1 and terminates with repeat 8. Residues in MCol1hC are numbered starting at the proline preceding the first cysteine, and the same numbering was used in the NMR structures. The highly conserved cysteine residues are marked in red. Proline in position 12, which is conserved with two exceptions, is marked in purple. The sequence of the synthesized and investigated peptide is underlined.

Figure 3.
FIG. 3. Stereo view of the same conformer as in Fig. 2 in ribbon presentation. Only structure 2 is shown. Cysteines and disulfide bonds are shown in yellow and Pro12 is in aquamarine. Disulfide bonds (Cys2-Cys18, Cys6-Cys14 and Cys10-Cys19) as well as the conserved Pro12 are indicated in ball-and-stick representation. Dashed lines indicate the hydrogen bonds identified by MOLMOL. These are bonds between Val5 (O) and Gln9 (HN), Val11 (O) and Cys14 (HN), and Pro15 (O) and Cys18 (HN). The first H-bond belongs to the -helix, others belong to the three different turns. Pro12 induces a I turn from residues 11 to 14. All proline residues in the structure can be shown to be in trans conformation from experimental nuclear Overhauser effect distance information.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2004, 279, 30395-30401) copyright 2004.

Figures were selected by the author.