2W6R

Crystal structure of an artificial (ba)8-barrel protein designed from identical half barrels

Summary for 2W6R

• Entry DOI: 10.2210/pdb2w6r/pdb
• Related: 1GPW 1THF 1VH7 2A0N
• Descriptor: IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF (2 entities in total)
• Functional Keywords: lyase, fusion protein, cobalamin, precorrin, novel fold, vitamin b12
• Biological source: THERMOTOGA MARITIMA
• Cellular location: Cytoplasm: Q9X0C6
• Total number of polymer chains: 1
• Total formula weight: 29611.17

Authors

Hocker, B.,Lochner, A.,Seitz, T.,Claren, J.,Sterner, R. (deposition date: 2008-12-18, release date: 2009-02-03, Last modification date: 2023-12-13)

Primary citation

Hocker, B.,Lochner, A.,Seitz, T.,Claren, J.,Sterner, R.
High-Resolution Crystal Structure of an Artificial (Betaalpha)(8)-Barrel Protein Designed from Identical Half-Barrels.
Biochemistry, 48:1145-, 2009

PubMed Abstract: Ample evidence suggests that the ubiquitous (betaalpha)(8)-barrel enzyme fold has evolved by the duplication and fusion of an ancestral (betaalpha)(4)-half-barrel. To reconstruct this process in the laboratory with a model protein, we earlier fused two copies of the C-terminal half-barrel HisF-C of imidazole glycerol phosphate synthase (HisF) and stepwise stabilized the resulting HisF-CC construct. We now further increased its stability and solubility by introducing two additional amino acid exchanges, which allowed us to crystallize the resulting artificial (betaalpha)(8)-barrel protein HisF-C***C. The analysis of its X-ray structure at 2.1 A resolution reveals a striking similarity to wild-type HisF, helps us to understand its improved stability, and provides further insights into the evolution of (betaalpha)(8)-barrel proteins.

PubMed: 19166324
DOI: 10.1021/BI802125B

Experimental method

X-RAY DIFFRACTION (2.1 Å)