PDBsum entry: 1prq

Contractile protein

PDB id: 1prq

Contents

Protein chain

125 a.a. *

Waters ×56

* Residue conservation analysis

PDB id:

1prq

Name:

Contractile protein

Title:

Acanthamoeba castellanii profilin ia

Structure:

Profilin ia. Chain: a. Engineered: yes

Source:

Acanthamoeba castellanii. Organism_taxid: 5755. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.50Å R-factor: 0.141

Authors:

A.A.Fedorov,T.D.Pollard,M.Way,E.E.Lattman,S.C.Almo

Key ref:

S.Liu et al. (1998). Crystal packing induces a conformational change in profilin-I from Acanthamoeba castellanii. J Struct Biol, 123, 22-29. PubMed id: 9774541 DOI: 10.1006/jsbi.1998.4009

Date:

18-Aug-97 Release date: 24-Dec-97

Protein chain

P68696  (PRO1A_ACACA) -  Profilin-1A

Seq: 126 a.a.

Struc: 125 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: cytoplasm (3 terms)
• Biological process: cytoskeleton organization (2 terms)
• Biochemical function: actin binding (2 terms)

DOI no: 10.1006/jsbi.1998.4009

J Struct Biol 123:22-29 (1998)

PubMed id: 9774541

Crystal packing induces a conformational change in profilin-I from Acanthamoeba castellanii.

S.Liu, A.A.Fedorov, T.D.Pollard, E.E.Lattman, S.C.Almo, K.A.Magnus.

ABSTRACT

Profilin-I from Acanthamoeba castellanii is a 13-kDa protein that binds actin and poly-l-proline. The native protein has been crystallized in two different but closely related forms. The second form proved more amenable to three-dimensional structural determination using heavy-atom isomorphous methods to obtain crystallographic phase information. We used the second crystal structure as a test molecule in the molecular replacement procedure to determine the structure of the first crystal form of profilin-I. More residues participate in crystal lattice contacts in the first crystal form than in the second. The two crystal forms differ significantly in the C-terminal helix that interacts with actin and in the loop preceding this helix. Coordinates of some main chain atoms here differ by about 1.0 A, and side chain atoms differ by more than 2.0 A.