1rz2
1.6A crystal structure of the protein BA4783/Q81L49 (similar to sortase B) from Bacillus anthracis.
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| , resolution 1.60Å | |||||||
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| Gene: | BA4783 (Bacillus anthracis str. Ames) | ||||||
| Domains: | COG4509 | ||||||
| Related: | 1NG5
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
Surface proteins attached by sortases to the cell wall envelope of bacterial pathogens play important roles during infection. Sorting and attachment of these proteins is directed by C-terminal signals. Sortase B of S. aureus recognizes a motif NPQTN, cleaves the polypeptide after the Thr residue, and attaches the protein to pentaglycine cross-bridges. Sortase B of B. anthracis is thought to recognize the NPKTG motif, and attaches surface proteins to m-diaminopimelic acid cross-bridges. We have determined crystal structure of sortase B from B. anthracis and S. aureus at 1.6 and 2.0 A resolutions, respectively. These structures show a beta-barrel fold with alpha-helical elements on its outside, a structure thus far exclusive to the sortase family. A putative active site located on the edge of the beta-barrel is comprised of a Cys-His-Asp catalytic triad and presumably faces the bacterial cell surface. A putative binding site for the sorting signal is located nearby.
About this StructureAbout this Structure
1RZ2 is a Single protein structure of sequence from Bacillus anthracis str. ames. Full crystallographic information is available from OCA.
ReferenceReference
Structures of sortase B from Staphylococcus aureus and Bacillus anthracis reveal catalytic amino acid triad in the active site., Zhang R, Wu R, Joachimiak G, Mazmanian SK, Missiakas DM, Gornicki P, Schneewind O, Joachimiak A, Structure. 2004 Jul;12(7):1147-56. PMID:15242591
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