User:Tilman Schirmer/Sandbox 203

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Revision as of 09:25, 15 July 2009 (edit) Tilman Schirmer (Talk | contribs) (→PlzD in complex with c-di-GMP) ← Previous diff		Revision as of 09:29, 15 July 2009 (edit) (undo) Tilman Schirmer (Talk | contribs) Next diff →
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		+	==References==
		+	PlzD structure [[1yln]]:
		+	<ref group="xtra">PMID:18366254</ref>
		+	<references group="xtra"/>
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		+	PlzD - c-di-GMP structure [[1rde]]:
		+	<ref group="xtra">PMID:18366254</ref>
		+	<references group="xtra"/>

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Revision as of 09:29, 15 July 2009

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C-di-GMP receptors with PilZ domain

PlzD

spinqualitylabelsall models PlzD 1yln Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

from Vibrio cholerae is composed of a and a C-terminal domain (with very similar fold).

The c-di-GMP is formed by arginine residues of the inter-domain linker and the PlzD domain surface .

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PlzD in complex with c-di-GMP

spinqualitylabelsall models PlzD 2rde Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Upon complex formation the relative domain arrangement is (compare with 1yln above), .

References

PlzD structure 1yln:

• De N, Pirruccello M, Krasteva PV, Bae N, Raghavan RV, Sondermann H. Phosphorylation-independent regulation of the diguanylate cyclase WspR. PLoS Biol. 2008 Mar 25;6(3):e67. PMID:18366254 doi:10.1371/journal.pbio.0060067

PlzD - c-di-GMP structure 1rde:

• De N, Pirruccello M, Krasteva PV, Bae N, Raghavan RV, Sondermann H. Phosphorylation-independent regulation of the diguanylate cyclase WspR. PLoS Biol. 2008 Mar 25;6(3):e67. PMID:18366254 doi:10.1371/journal.pbio.0060067