PDBsum entry 4mn0

Luminescent protein

PDB id: 4mn0

Contents

Protein chain

182 a.a.

Metals

_MG

_CA ×3

Waters ×180

PDB id:

4mn0

Name:

Luminescent protein

Title:

Spatial structure of the novel light-sensitive photoprotein berovin from the ctenophore beroe abyssicola in the ca2+-loaded apoprotein conformation state

Structure:

Berovin. Chain: a. Synonym: apoberovin. Engineered: yes

Source:

Beroe abyssicola. Organism_taxid: 320166. Gene: ba2, ba1, ba3, ba4. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.90Å R-factor: 0.196 R-free: 0.256

Authors:

Z.J.Liu,G.A.Stepanyuk,E.S.Vysotski,J.Lee,J.P.Rose,B.C.Wang,Southeast Collaboratory For Structural Genomics (Secsg)

Key ref:

G.A.Stepanyuk et al. (2013). Spatial structure of the novel light-sensitive photoprotein berovin from the ctenophore Beroe abyssicola in the Ca(2+)-loaded apoprotein conformation state. Biochim Biophys Acta, 1834, 2139-2146. PubMed id: 23891746 DOI: 10.1016/j.bbapap.2013.07.006

Date:

09-Sep-13 Release date: 16-Oct-13

Supersedes:

2hpk

Protein chain

H8ZZK1  (H8ZZK1_BERAB) -  Apoberovin 1 from Beroe abyssicola

Seq: 208 a.a.

Struc: 182 a.a.

DOI no: 10.1016/j.bbapap.2013.07.006

Biochim Biophys Acta 1834:2139-2146 (2013)

PubMed id: 23891746

Spatial structure of the novel light-sensitive photoprotein berovin from the ctenophore Beroe abyssicola in the Ca(2+)-loaded apoprotein conformation state.

G.A.Stepanyuk, Z.J.Liu, L.P.Burakova, J.Lee, J.Rose, E.S.Vysotski, B.C.Wang.

ABSTRACT

The bright bioluminescence of ctenophores, found in oceans worldwide, is determined by Ca(2+)-regulated photoproteins, functionally identical to and sharing many properties of hydromedusan photoproteins. In contrast, however, the ctenophore photoproteins are extremely sensitive to UV and visible light over the range of their absorption spectrum. The spatial structure of a novel light-sensitive photoprotein from the ctenophore Beroe abyssicola in its apoform bound with three calcium ions is determined at 2.0Å. We demonstrate that the apoberovin is a slightly asymmetrical compact globular protein formed by two domains with a cavity in the center, which exactly retains the fold architecture characteristic of hydromedusan photoproteins despite their low amino acid sequence identity. However, the structural alignment of these two photoprotein classes clearly shows that despite the high similarity of shape and geometry of their coelenterazine-binding cavities, their interiors differ drastically. The key residues appearing to be crucial for stabilizing the 2-hydroperoxycoelenterazine and for formation of the emitter in hydromedusan photoproteins, are replaced in berovin by amino acid residues having completely different side chain properties. Evidently, these replacements must be responsible for the distinct properties of ctenophore photoproteins such as sensitivity to light or the fact that the formation of active photoprotein from apophotoprotein, coelenterazine, and oxygen is more effective at alkaline pH.