1ng5
From Proteopedia
(New page: 200px<br /><applet load="1ng5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ng5, resolution 2.00Å" /> '''2.0 A crystal struct...) |
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| - | [[Image:1ng5.gif|left|200px]]<br /><applet load="1ng5" size=" | + | [[Image:1ng5.gif|left|200px]]<br /><applet load="1ng5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ng5, resolution 2.00Å" /> | caption="1ng5, resolution 2.00Å" /> | ||
'''2.0 A crystal structure of Staphylococcus aureus Sortase B'''<br /> | '''2.0 A crystal structure of Staphylococcus aureus Sortase B'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Surface proteins attached by sortases to the cell wall envelope of | + | 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 Structure== | ==About this Structure== | ||
| - | 1NG5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus Staphylococcus aureus subsp. aureus]. Full crystallographic information is available from [http:// | + | 1NG5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus Staphylococcus aureus subsp. aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NG5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Joachimiak, A.]] | [[Category: Joachimiak, A.]] | ||
[[Category: Joachimiak, G.]] | [[Category: Joachimiak, G.]] | ||
| - | [[Category: MCSG, Midwest | + | [[Category: MCSG, Midwest Center for Structural Genomics.]] |
[[Category: Zhang, R.]] | [[Category: Zhang, R.]] | ||
[[Category: a new fold]] | [[Category: a new fold]] | ||
| Line 24: | Line 24: | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:41 2008'' |
Revision as of 12:05, 21 February 2008
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2.0 A crystal structure of Staphylococcus aureus Sortase B
Overview
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 Structure
1NG5 is a Single protein structure of sequence from Staphylococcus aureus subsp. aureus. Full crystallographic information is available from OCA.
Reference
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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