PDBsum entry 1ypr

Actin-binding protein

PDB id

1ypr

Loading ...

Contents

			Protein chains

					125 a.a. *

			Waters ×39

* Residue conservation analysis

PDB id:

1ypr

Links

Name:

Actin-binding protein

Title:

Saccharomyces cerevisiae (yeast) profilin

Structure:

Profilin. Chain: a, b. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.30Å

R-factor:

0.168

R-free:

0.220

Authors:

J.C.Eads,N.M.Mahoney,S.C.Almo

Key ref:

J.C.Eads et al. (1998). Structure determination and characterization of Saccharomyces cerevisiae profilin. Biochemistry, 37, 11171-11181. PubMed id: 9698363 DOI: 10.1021/bi9720033

Date:

26-Jun-97

Release date:

31-Dec-97

PROCHECK

	Headers

	References

Protein chains

P07274 (PROF_YEAST) - Profilin from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: Struc:					126 a.a. 125 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1021/bi9720033	Biochemistry 37:11171-11181 (1998)
PubMed id: 9698363

Structure determination and characterization of Saccharomyces cerevisiae profilin.
J.C.Eads, N.M.Mahoney, S.Vorobiev, A.R.Bresnick, K.K.Wen, P.A.Rubenstein, B.K.Haarer, S.C.Almo.

ABSTRACT

The structure of profilin from the budding yeast Saccharomyces cerevisiae has been determined by X-ray crystallography at 2.3 A resolution. The overall fold of yeast profilin is similar to the fold observed for other profilin structures. The interactions of yeast and human platelet profilins with rabbit skeletal muscle actin were characterized by titration microcalorimetry, fluorescence titrations, and nucleotide exchange kinetics. The affinity of yeast profilin for rabbit actin (2.9 microM) is approximately 30-fold weaker than the affinity of human platelet profilin for rabbit actin (0.1 microM), and the relative contributions of entropic and enthalpic terms to the overall free energy of binding are different for the two profilins. The titration of pyrene-labeled rabbit skeletal actin with human profilin yielded a Kd of 2.8 microM, similar to the Kd of 2.0 microM for the interaction between yeast profilin and pyrene-labeled yeast actin. The binding data are discussed in the context of the known crystal structures of profilin and actin, and the residues present at the actin-profilin interface. The affinity of yeast profilin for poly-L-proline was determined from fluorescence measurements and is similar to the reported affinity of Acanthamoeba profilin for poly-L-proline. Yeast profilin was shown to catalyze adenine nucleotide exchange from yeast actin almost 2 orders of magnitude less efficiently than human profilin and rabbit skeletal muscle actin. The in vivo and in vitro properties of yeast profilin mutants with altered poly-L-proline and actin binding sites are discussed in the context of the crystal structure.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20148388

K.Ueno, Y.Tamura, and H.Chibana (2010).
Target validation and ligand development for a pathogenic fungal profilin, using a knock-down strain of pathogenic yeast Candida glabrata and structure-based ligand design.

Yeast, 27, 369-378.

19251693

A.S.Paul, and T.D.Pollard (2009).
Energetic Requirements for Processive Elongation of Actin Filaments by FH1FH2-formins.

J Biol Chem, 284, 12533-12540.

19450534

M.Gandhi, V.Achard, L.Blanchoin, and B.L.Goode (2009).
Coronin switches roles in actin disassembly depending on the nucleotide state of actin.

Mol Cell, 34, 364-374.

19028693

O.C.Ezezika, N.S.Younger, J.Lu, D.A.Kaiser, Z.A.Corbin, B.J.Nolen, D.R.Kovar, and T.D.Pollard (2009).
Incompatibility with Formin Cdc12p Prevents Human Profilin from Substituting for Fission Yeast Profilin: INSIGHTS FROM CRYSTAL STRUCTURES OF FISSION YEAST PROFILIN.

J Biol Chem, 284, 2088-2097.

PDB codes:

3d9y 3dav

19289059

R.Kardos, K.Pozsonyi, E.Nevalainen, P.Lappalainen, M.Nyitrai, and G.Hild (2009).
The effects of ADF/cofilin and profilin on the conformation of the ATP-binding cleft of monomeric actin.

Biophys J, 96, 2335-2343.

18160294

A.S.Paul, A.Paul, T.D.Pollard, and T.Pollard (2008).
The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation.

Curr Biol, 18, 9.

18305104

A.Yonetani, R.J.Lustig, J.B.Moseley, T.Takeda, B.L.Goode, and F.Chang (2008).
Regulation and targeting of the fission yeast formin cdc12p in cytokinesis.

Mol Biol Cell, 19, 2208-2219.

19000816

I.Kursula, P.Kursula, M.Ganter, S.Panjikar, K.Matuschewski, and H.Schüler (2008).
Structural basis for parasite-specific functions of the divergent profilin of Plasmodium falciparum.

Structure, 16, 1638-1648.

PDB codes:

2jkf 2jkg

18223293

K.K.Wen, M.McKane, J.C.Houtman, and P.A.Rubenstein (2008).
Control of the ability of profilin to bind and facilitate nucleotide exchange from G-actin.

J Biol Chem, 283, 9444-9453.

17538023

F.Chaudhry, C.Guérin, M.von Witsch, L.Blanchoin, and C.J.Staiger (2007).
Identification of Arabidopsis cyclase-associated protein 1 as the first nucleotide exchange factor for plant actin.

Mol Biol Cell, 18, 3002-3014.

16317718

D.Polet, A.Lambrechts, K.Ono, A.Mah, F.Peelman, J.Vandekerckhove, D.L.Baillie, C.Ampe, and S.Ono (2006).
Caenorhabditis elegans expresses three functional profilins in a tissue-specific manner.

Cell Motil Cytoskeleton, 63, 14-28.

16483928

D.Vavylonis, D.R.Kovar, B.O'Shaughnessy, and T.D.Pollard (2006).
Model of formin-associated actin filament elongation.

Mol Cell, 21, 455-466.

16959963

J.B.Moseley, and B.L.Goode (2006).
The yeast actin cytoskeleton: from cellular function to biochemical mechanism.

Microbiol Mol Biol Rev, 70, 605-645.

16611742

K.Okada, H.Ravi, E.M.Smith, and B.L.Goode (2006).
Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: a coordinated mechanism for severing and capping filaments.

Mol Biol Cell, 17, 2855-2868.

15923184

J.B.Moseley, and B.L.Goode (2005).
Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6.

J Biol Chem, 280, 28023-28033.

16118223

M.McKane, K.K.Wen, I.R.Boldogh, S.Ramcharan, L.A.Pon, and P.A.Rubenstein (2005).
A mammalian actin substitution in yeast actin (H372R) causes a suppressible mitochondria/vacuole phenotype.

J Biol Chem, 280, 36494-36501.

14657240

J.B.Moseley, I.Sagot, A.L.Manning, Y.Xu, M.J.Eck, D.Pellman, and B.L.Goode (2004).
A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin.

Mol Biol Cell, 15, 896-907.

15548863

K.K.Wen, M.S.Blake, and P.A.Rubenstein (2004).
Neisseria gonorrhoeae porin, P.IB, causes release of ATP from yeast actin.

J Muscle Res Cell Motil, 25, 343-350.

12814545

A.A.Rodal, A.L.Manning, B.L.Goode, and D.G.Drubin (2003).
Negative regulation of yeast WASp by two SH3 domain-containing proteins.

Curr Biol, 13, 1000-1008.

12529431

R.Hopmann, and K.G.Miller (2003).
A balance of capping protein and profilin functions is required to regulate actin polymerization in Drosophila bristle.

Mol Biol Cell, 14, 118-128.

11294914

J.Lu, and T.D.Pollard (2001).
Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast.

Mol Biol Cell, 12, 1161-1175.

10953013

A.K.Wolven, L.D.Belmont, N.M.Mahoney, S.C.Almo, and D.G.Drubin (2000).
In vivo importance of actin nucleotide exchange catalyzed by profilin.

J Cell Biol, 150, 895-904.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.