1psz
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(New page: 200px<br /><applet load="1psz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1psz, resolution 2.0Å" /> '''PNEUMOCOCCAL SURFACE ...)
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Revision as of 21:58, 20 November 2007
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PNEUMOCOCCAL SURFACE ANTIGEN PSAA
Overview
Background:. The surface protein PsaA of the pathogenic bacterium, Streptococcus pneumoniae plays an essential role in its virulence. PsaA is, a putative ATP-binding cassette-type (ABC-type) binding protein involved, in the uptake of Mn2+ and possibly Zn2+ and is considered to be both a, potential drug target and and a candidate vaccine component. Results:. The, structure of PsaA has been determined to 2.0 A resolution using X-ray, crystallography and is the first structure obtained for an ABC-type, binding protein from a Gram-positive organism. The protein consists of two, (beta/alpha)4 domains linked together by a single helix. A metal-binding, site is formed in the domain interface by the sidechains of His67, His139, Glu205 and Asp280 and is occupied in the structure. Conclusions:. The, structural topology of PsaA is fundamentally different from that of other, ABC-type binding proteins determined thus far in that PsaA lacks the, characteristic 'hinge peptides' involved in conformational change upon, solute uptake and release. In our structure, the metal-binding site is, probably occupied by Zn2+. The site seems to be well conserved amongst, related receptors from both Gram-positive and Gram-negative bacteria.
About this Structure
1PSZ is a Single protein structure of sequence from Streptococcus pneumoniae with ZN as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure for a putative ABC-type binding protein., Lawrence MC, Pilling PA, Epa VC, Berry AM, Ogunniyi AD, Paton JC, Structure. 1998 Dec 15;6(12):1553-61. PMID:9862808
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