1sxr
From Proteopedia
(New page: 200px<br /><applet load="1sxr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sxr, resolution 1.56Å" /> '''Drosophila Peptidogl...) |
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| - | [[Image:1sxr.gif|left|200px]]<br /><applet load="1sxr" size=" | + | [[Image:1sxr.gif|left|200px]]<br /><applet load="1sxr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sxr, resolution 1.56Å" /> | caption="1sxr, resolution 1.56Å" /> | ||
'''Drosophila Peptidoglycan Recognition Protein (PGRP)-SA'''<br /> | '''Drosophila Peptidoglycan Recognition Protein (PGRP)-SA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Peptidoglycan recognition proteins (PGRPs) form a recently discovered | + | Peptidoglycan recognition proteins (PGRPs) form a recently discovered protein family, which is conserved from insect to mammals and is implicated in the innate immune system by interacting with/or degrading microbial peptidoglycans (PGNs). Drosophila PGRP-SA is a member of this family of pattern recognition receptors and is involved in insect Toll activation. We report here the crystal structure of PGRP-SA at 1.56 A resolution, which represents the first example of a "recognition" PGRP. Comparison with the catalytic Drosophila PGRP-LB reveals an overall structure conservation with an L-shaped hydrophilic groove that is likely the PGN carbohydrate core binding site, but further suggests some possible functional homology between recognition and catalytic PGRPs. Consistent with sequence analysis, PGRP-SA does not contain the canonical zinc-binding residues found in catalytic PGRPs. However, substitution of the zinc-binding cysteine residue by serine, along with an altered coordinating histidine residue, assembles a constellation of residues that resembles a modified catalytic triad. The serine/histidine juxtaposition to a threonine residue and a carbonyl oxygen atom, along with conservation of the catalytic water molecule found in PGRP-LB, tantalizingly suggests some hydrolytic function for this member of receptor PGRPs. |
==About this Structure== | ==About this Structure== | ||
| - | 1SXR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with SO4 and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1SXR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SXR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Reiser, J | + | [[Category: Reiser, J B.]] |
[[Category: Teyton, L.]] | [[Category: Teyton, L.]] | ||
| - | [[Category: Wilson, I | + | [[Category: Wilson, I A.]] |
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: toll pathway]] | [[Category: toll pathway]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:06:44 2008'' |
Revision as of 13:06, 21 February 2008
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Drosophila Peptidoglycan Recognition Protein (PGRP)-SA
Overview
Peptidoglycan recognition proteins (PGRPs) form a recently discovered protein family, which is conserved from insect to mammals and is implicated in the innate immune system by interacting with/or degrading microbial peptidoglycans (PGNs). Drosophila PGRP-SA is a member of this family of pattern recognition receptors and is involved in insect Toll activation. We report here the crystal structure of PGRP-SA at 1.56 A resolution, which represents the first example of a "recognition" PGRP. Comparison with the catalytic Drosophila PGRP-LB reveals an overall structure conservation with an L-shaped hydrophilic groove that is likely the PGN carbohydrate core binding site, but further suggests some possible functional homology between recognition and catalytic PGRPs. Consistent with sequence analysis, PGRP-SA does not contain the canonical zinc-binding residues found in catalytic PGRPs. However, substitution of the zinc-binding cysteine residue by serine, along with an altered coordinating histidine residue, assembles a constellation of residues that resembles a modified catalytic triad. The serine/histidine juxtaposition to a threonine residue and a carbonyl oxygen atom, along with conservation of the catalytic water molecule found in PGRP-LB, tantalizingly suggests some hydrolytic function for this member of receptor PGRPs.
About this Structure
1SXR is a Single protein structure of sequence from Drosophila melanogaster with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Drosophila peptidoglycan recognition protein (PGRP)-SA at 1.56 A resolution., Reiser JB, Teyton L, Wilson IA, J Mol Biol. 2004 Jul 16;340(4):909-17. PMID:15223330
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