1psz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1psz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1psz, resolution 2.0&Aring;" /> '''PNEUMOCOCCAL SURFACE ...)
Line 1: Line 1:
-
[[Image:1psz.gif|left|200px]]<br /><applet load="1psz" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1psz.gif|left|200px]]<br /><applet load="1psz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1psz, resolution 2.0&Aring;" />
caption="1psz, resolution 2.0&Aring;" />
'''PNEUMOCOCCAL SURFACE ANTIGEN PSAA'''<br />
'''PNEUMOCOCCAL SURFACE ANTIGEN PSAA'''<br />
==Overview==
==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.
+
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==
==About this Structure==
-
1PSZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PSZ OCA].
+
1PSZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PSZ OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptococcus pneumoniae]]
[[Category: Streptococcus pneumoniae]]
-
[[Category: Berry, A.M.]]
+
[[Category: Berry, A M.]]
-
[[Category: Epa, V.C.]]
+
[[Category: Epa, V C.]]
-
[[Category: Lawrence, M.C.]]
+
[[Category: Lawrence, M C.]]
-
[[Category: Ogunniyi, A.D.]]
+
[[Category: Ogunniyi, A D.]]
-
[[Category: Paton, J.C.]]
+
[[Category: Paton, J C.]]
-
[[Category: Pilling, P.A.]]
+
[[Category: Pilling, P A.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: abc-type binding protein]]
[[Category: abc-type binding protein]]
Line 25: Line 25:
[[Category: psaa]]
[[Category: psaa]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:05:50 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:16 2008''

Revision as of 12:32, 21 February 2008


1psz, resolution 2.0Å

Drag the structure with the mouse to rotate

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 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

Page seeded by OCA on Thu Feb 21 14:32:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools