2NZO

Crystal structure of a secretion chaperone CsaA from Bacillus subtilis in the space group P 32 2 1

Summary for 2NZO

• Entry DOI: 10.2210/pdb2nzo/pdb
• Related: 2NZH
• Descriptor: Protein csaA, GLYCEROL (3 entities in total)
• Functional Keywords: beta barrel, oligonucleotide/oligosaccharide binding fold, ob fold, homodimer, chaperone
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm (Probable): P37584
• Total number of polymer chains: 4
• Total formula weight: 49365.15

Authors

Shapova, Y.A.,Paetzel, M. (deposition date: 2006-11-24, release date: 2007-03-27, Last modification date: 2023-08-30)

Primary citation

Shapova, Y.A.,Paetzel, M.
Crystallographic analysis of Bacillus subtilis CsaA.
Acta Crystallogr.,Sect.D, 63:478-485, 2007

PubMed Abstract: Bacillus subtilis CsaA (BsCsaA) has been proposed to act as a protein-secretion chaperone in the Sec-dependent translocation pathway, possibly compensating for the lack of SecB in the Gram-positive eubacterium Bacillus subtilis. This paper presents the cloning, purification, crystallization and structures of BsCsaA in two space groups (P42(1)2 and P3(2)21) solved and refined to resolutions of 1.9 and 2.0 A, respectively. These structures complement the previously available crystal structure of CsaA from the Gram-negative eubacterium Thermus thermophilus (TtCsaA) and provide a direct structural basis for the interpretation of previously available biochemical data on BsCsaA. The sequence and structure of the proposed substrate-binding pocket are analyzed and discussed. A comparison with the TtCsaA structure reveals a different pattern of electrostatic potential in the vicinity of the binding site, which overlaps with a region of high sequence variability. In addition, the dimerization interface of this homodimeric protein is analyzed and discussed.

PubMed: 17372352
DOI: 10.1107/S0907444907005045

Experimental method

X-RAY DIFFRACTION (2 Å)