1ng5: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE= SA0982 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46170 Staphylococcus aureus subsp. aureus])
|GENE= SA0982 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46170 Staphylococcus aureus subsp. aureus])
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG4509 COG4509]</span>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ng5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ng5 OCA], [http://www.ebi.ac.uk/pdbsum/1ng5 PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1ng5 RCSB]</span>
}}
}}


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[[Category: structural genomic]]
[[Category: structural genomic]]


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Revision as of 06:58, 26 March 2008

File:1ng5.gif


PDB ID 1ng5

Drag the structure with the mouse to rotate
, resolution 2.00Å
Gene: SA0982 (Staphylococcus aureus subsp. aureus)
Domains: COG4509
Resources: FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates: save as pdb, mmCIF, xml



2.0 A crystal structure of Staphylococcus aureus Sortase B


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

1NG5 is a Single protein structure of sequence from Staphylococcus aureus subsp. aureus. 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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