2pil
From Proteopedia
(New page: 200px<br /><applet load="2pil" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pil, resolution 2.6Å" /> '''CRYSTALLOGRAPHIC STRU...) |
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| - | [[Image:2pil.gif|left|200px]]<br /><applet load="2pil" size=" | + | [[Image:2pil.gif|left|200px]]<br /><applet load="2pil" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2pil, resolution 2.6Å" /> | caption="2pil, resolution 2.6Å" /> | ||
'''CRYSTALLOGRAPHIC STRUCTURE OF PHOSPHORYLATED PILIN FROM NEISSERIA: PHOSPHOSERINE SITES MODIFY TYPE IV PILUS SURFACE CHEMISTRY'''<br /> | '''CRYSTALLOGRAPHIC STRUCTURE OF PHOSPHORYLATED PILIN FROM NEISSERIA: PHOSPHOSERINE SITES MODIFY TYPE IV PILUS SURFACE CHEMISTRY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Understanding the structural biology of type IV pili, fibres responsible | + | Understanding the structural biology of type IV pili, fibres responsible for the virulent attachment and motility of numerous bacterial pathogens, requires a detailed understanding of the three-dimensional structure and chemistry of the constituent pilin subunit. X-ray crystallographic refinement of Neisseria gonorrhoeae pilin against diffraction data to 2.6 A resolution, coupled with mass spectrometry of peptide fragments, reveals phosphoserine at residue 68. Phosphoserine is exposed on the surface of the modelled type IV pilus at the interface of neighbouring pilin molecules. The site-specific mutation of serine 68 to alanine showed that the loss of the phosphorylation alters the morphology of fibres examined by electron microscopy without a notable effect on adhesion, transformation, piliation or twitching motility. The structural and chemical characterization of protein phosphoserine in type IV pilin subunits is an important indication that this modification, key to numerous regulatory aspects of eukaryotic cell biology, exists in the virulence factor proteins of bacterial pathogens. These O-linked phosphate modifications, unusual in prokaryotes, thus merit study for possible roles in pilus biogenesis and modulation of pilin chemistry for optimal in vivo function. |
==About this Structure== | ==About this Structure== | ||
| - | 2PIL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae] with PT and HTO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2PIL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae] with <scene name='pdbligand=PT:'>PT</scene> and <scene name='pdbligand=HTO:'>HTO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PIL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Neisseria gonorrhoeae]] | [[Category: Neisseria gonorrhoeae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dunham, S | + | [[Category: Dunham, S A.]] |
| - | [[Category: Forest, K | + | [[Category: Forest, K T.]] |
[[Category: Koomey, M.]] | [[Category: Koomey, M.]] | ||
| - | [[Category: Tainer, J | + | [[Category: Tainer, J A.]] |
[[Category: HTO]] | [[Category: HTO]] | ||
[[Category: PT]] | [[Category: PT]] | ||
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[[Category: type 4 pilin]] | [[Category: type 4 pilin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:29:47 2008'' |
Revision as of 16:29, 21 February 2008
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CRYSTALLOGRAPHIC STRUCTURE OF PHOSPHORYLATED PILIN FROM NEISSERIA: PHOSPHOSERINE SITES MODIFY TYPE IV PILUS SURFACE CHEMISTRY
Overview
Understanding the structural biology of type IV pili, fibres responsible for the virulent attachment and motility of numerous bacterial pathogens, requires a detailed understanding of the three-dimensional structure and chemistry of the constituent pilin subunit. X-ray crystallographic refinement of Neisseria gonorrhoeae pilin against diffraction data to 2.6 A resolution, coupled with mass spectrometry of peptide fragments, reveals phosphoserine at residue 68. Phosphoserine is exposed on the surface of the modelled type IV pilus at the interface of neighbouring pilin molecules. The site-specific mutation of serine 68 to alanine showed that the loss of the phosphorylation alters the morphology of fibres examined by electron microscopy without a notable effect on adhesion, transformation, piliation or twitching motility. The structural and chemical characterization of protein phosphoserine in type IV pilin subunits is an important indication that this modification, key to numerous regulatory aspects of eukaryotic cell biology, exists in the virulence factor proteins of bacterial pathogens. These O-linked phosphate modifications, unusual in prokaryotes, thus merit study for possible roles in pilus biogenesis and modulation of pilin chemistry for optimal in vivo function.
About this Structure
2PIL is a Single protein structure of sequence from Neisseria gonorrhoeae with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystallographic structure reveals phosphorylated pilin from Neisseria: phosphoserine sites modify type IV pilus surface chemistry and fibre morphology., Forest KT, Dunham SA, Koomey M, Tainer JA, Mol Microbiol. 1999 Feb;31(3):743-52. PMID:10048019
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