PDBsum entry 2o31

Signaling protein

PDB id: 2o31

Contents

Protein chain

67 a.a. *

Ligands

FMT ×2

Waters ×101

* Residue conservation analysis

PDB id:

2o31

Name:

Signaling protein

Title:

Crystal structure of the second sh3 domain from ponsin

Structure:

Ponsin. Chain: a. Fragment: src homology 3 (sh3) domain. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: sorbs1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.50Å R-factor: 0.132 R-free: 0.162

Authors:

N.Pinotsis,M.Wilmanns,I.Margiolaki

Key ref:

I.Margiolaki et al. (2007). Second SH3 domain of ponsin solved from powder diffraction. J Am Chem Soc, 129, 11865-11871. PubMed id: 17784760

Date:

30-Nov-06 Release date: 23-Oct-07

Protein chain

Q9BX66  (SRBS1_HUMAN) -  Sorbin and SH3 domain-containing protein 1 from Homo sapiens

Seq: 1292 a.a.

Struc: 67 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

J Am Chem Soc 129:11865-11871 (2007)

PubMed id: 17784760

Second SH3 domain of ponsin solved from powder diffraction.

I.Margiolaki, J.P.Wright, M.Wilmanns, A.N.Fitch, N.Pinotsis.

ABSTRACT

Determination of protein crystal structures is dependent on the growth of high-quality single crystals, a process that is not always successful. Optimum crystallization conditions must be systematically sought for, and microcrystalline powders are frequently obtained in failed attempts to grow the desired crystal. In materials science, structures of samples ranging from ceramics, pharmaceuticals, zeolites, etc., can nowadays be solved, almost routinely, from powdered samples, and there seems to be no fundamental reason, except the sheer size and complexity of the structures involved, why powder diffraction should not be employed to solve structures of small proteins. Indeed, recent work has shown that the high-quality powder diffraction data can be used in the study of protein crystal structures. We report the solution, model building, and refinement of a 67-residue protein domain crystal structure, with a cell volume of 64 879 A3, from powder diffraction. The second SH3 domain of ponsin, a protein of high biological significance due to its role in cellular processes, is determined and refined to resolution limits comparable to single-crystal techniques. Our results demonstrate the power and future applicability of the powder technique in structural biology.