ISDA: 1M5Q

Deposition Date 2002-07-09

Release Date 2003-03-18

Last Version Date 2024-10-30

Entry Detail

PDB ID:

1M5Q

Keywords:

TRANSLATION

Title:

Crystal structure of a novel Sm-like archaeal protein from Pyrobaculum aerophilum

Biological Source:

Source Organism(s):

Pyrobaculum aerophilum (Taxon ID: 13773)

Expression System(s):

Escherichia coli bl21(de3)

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.00 Å

R-Value Free:

0.23

R-Value Work:

0.19

R-Value Observed:

0.19

Space Group:

P 1 21 1

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:small nuclear ribonucleoprote
Gene (Uniprot):PAE2122
Chain IDs:A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, AA (auth: 1), BA (auth: 2)
Chain Length:130
Number of Molecules:28
Biological Source:Pyrobaculum aerophilum

UniProt ID:Q8ZVU2 Pfam ID:PF14438, PF14894

Modified Residue

Compound ID	Chain ID	Parent Comp ID	Details	2D Image
MSE	A	MET	SELENOMETHIONINE

Ligand Molecules

ACY

GOL

Primary Citation

Structure and assembly of an augmented Sm-like archaeal protein 14-mer

Mura, C, Phillips, M, Kozhukhovsky, A, Eisenberg, D.Show

Proc. Natl. Acad. Sci. U.S.A. 100 4539 4544 (2003)

PMID: 12668760 DOI: 10.1073/pnas.0538042100

Abstact

To better understand the roles of Sm proteins in forming the cores of many RNA-processing ribonucleoproteins, we determined the crystal structure of an atypical Sm-like archaeal protein (SmAP3) in which the conserved Sm domain is augmented by a previously uncharacterized, mixed alpha/beta C-terminal domain. The structure reveals an unexpected SmAP3 14-mer that is perforated by a cylindrical pore and is bound to 14 cadmium (Cd(2+)) ions. Individual heptamers adopt either "apical" or "equatorial" conformations that chelate Cd(2+) differently. SmAP3 forms supraheptameric oligomers (SmAP3)(n = 7,14,28) in solution, and assembly of the asymmetric 14-mer is modulated by differential divalent cation-binding in apical and equatorial subunits. Phylogenetic and sequence analyses substantiate SmAP3s as a unique subset of SmAPs. These results distinguish SmAP3s from other Sm proteins and provide a model for the structure and properties of Sm proteins >100 residues in length, e.g., several human Sm proteins.

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Primary Citation of related structures

Abstact

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