1rz2: Difference between revisions

Revision as of 06:48, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1rz2.png

Template:STRUCTURE 1rz2

1.6A crystal structure of the protein BA4783/Q81L49 (similar to sortase B) from Bacillus anthracis.1.6A crystal structure of the protein BA4783/Q81L49 (similar to sortase B) from Bacillus anthracis.

Template:ABSTRACT PUBMED 15242591

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

Page seeded by OCA on Mon Jul 28 06:48:03 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''1.6A crystal structure of the protein BA4783/Q81L49 (similar to sortase B) from Bacillus anthracis.'''
+===1.6A crystal structure of the protein BA4783/Q81L49 (similar to sortase B) from Bacillus anthracis.===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15242591}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15242591}}
 ==About this Structure==
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 [[Category: Sortase b protein]]
 [[Category: Structural genomic]]
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