PDBsum entry 1psr

Ef-hand protein

PDB id: 1psr

Contents

Protein chains

100 a.a. *

Metals

_HO ×2

Waters ×387

* Residue conservation analysis

PDB id:

1psr

Name:

Ef-hand protein

Title:

Human psoriasin (s100a7)

Structure:

Psoriasin. Chain: a, b. Synonym: s100a7. Engineered: yes. Other_details: ca2+ substituted for ho3+

Source:

Homo sapiens. Human. Organism_taxid: 9606. Tissue: keratinocytes. Cellular_location: cytoplasmic or may be secreted by a non-classical secretory pathway. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Biol. unit:

Dimer (from PQS)

Resolution:

1.05Å R-factor: 0.109 R-free: 0.141

Authors:

D.E.Brodersen,M.Etzerodt,P.Madsen,J.Celis,H.C.Thoegersen,J.Nyborg, M.Kjeldgaard

Key ref:

D.E.Brodersen et al. (1998). EF-hands at atomic resolution: the structure of human psoriasin (S100A7) solved by MAD phasing. Structure, 6, 477-489. PubMed id: 9562557 DOI: 10.1016/S0969-2126(98)00049-5

Date:

27-Nov-97 Release date: 13-Jan-99

Protein chains

P31151  (S10A7_HUMAN) -  Protein S100-A7 from Homo sapiens

Seq: 101 a.a.

Struc: 100 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1016/S0969-2126(98)00049-5

Structure 6:477-489 (1998)

PubMed id: 9562557

EF-hands at atomic resolution: the structure of human psoriasin (S100A7) solved by MAD phasing.

D.E.Brodersen, M.Etzerodt, P.Madsen, J.E.Celis, H.C.Thøgersen, J.Nyborg, M.Kjeldgaard.

ABSTRACT

BACKGROUND: The S100 family consists of small acidic proteins, belonging to the EF-hand class of calcium-binding proteins. They are primarily regulatory proteins, involved in cell growth, cell structure regulation and signal transduction. Psoriasin (S100A7) is an 11.7 kDa protein that is highly upregulated in the epidermis of patients suffering from the chronic skin disease psoriasis. Although its exact function is not known, psoriasin is believed to participate in the biochemical response which follows transient changes in the cellular Ca2+ concentration. RESULTS: The three-dimensional structure of holmium-substituted psoriasin has been determined by multiple anomalous wavelength dispersion (MAD) phasing and refined to atomic resolution (1.05 A). The structure represents the most accurately determined structure of a calcium-binding protein. Although the overall structure of psoriasin is similar to those of other S100 proteins, several important differences exist, mainly in the N-terminal EF-hand motif that contains a distorted loop and lacks a crucial calcium-binding residue. It is these minor differences that may account for the different specificities among members of this family. CONCLUSIONS: The structure of human psoriasin reveals that this protein, in contrast to other S100 proteins with known structure, is not likely to strongly bind more than one calcium ion per monomer. The present study contradicts the idea that calcium binding induces large changes in conformation, as suggested by previously determined structures of apo forms of S100 proteins. The substitution of Ca2+ ions in EF-hands by lanthanide ions may provide a general vehicle for structure determination of S100 proteins by means of MAD phasing.

Selected figure(s)

Figure 7.
Figure 7. The Ramachandran plot for the final model. Non-glycine and non-proline residues are indicated by solid circles (asparagine residues as solid diamonds) and glycine residues as open squares. The shaded area corresponds to the 98% core regions as defined by Kleywegt and Jones [38]. Plot was created with rama (MK, unpublished program).

The above figure is reprinted by permission from Cell Press: Structure (1998, 6, 477-489) copyright 1998.

Figure was selected by an automated process.