2rde
From Proteopedia
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{{STRUCTURE_2rde| PDB=2rde | SCENE= }} | {{STRUCTURE_2rde| PDB=2rde | SCENE= }} | ||
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===Crystal structure of VCA0042 complexed with c-di-GMP=== | ===Crystal structure of VCA0042 complexed with c-di-GMP=== | ||
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{{ABSTRACT_PUBMED_18034161}} | {{ABSTRACT_PUBMED_18034161}} | ||
==About this Structure== | ==About this Structure== | ||
| - | [[2rde]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[2rde]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae_o395 Vibrio cholerae o395]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RDE OCA]. |
==See Also== | ==See Also== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:018034161</ref><references group="xtra"/> | <ref group="xtra">PMID:018034161</ref><references group="xtra"/> | ||
| - | [[Category: Vibrio cholerae]] | + | [[Category: Vibrio cholerae o395]] |
[[Category: Benach, J.]] | [[Category: Benach, J.]] | ||
[[Category: Camilli, A.]] | [[Category: Camilli, A.]] | ||
Revision as of 11:02, 11 March 2013
Contents |
Crystal structure of VCA0042 complexed with c-di-GMP
The second messenger cyclic diguanylate (c-di-GMP) controls the transition between motile and sessile growth in eubacteria, but little is known about the proteins that sense its concentration. Bioinformatics analyses suggested that PilZ domains bind c-di-GMP and allosterically modulate effector pathways. We have determined a 1.9 A crystal structure of c-di-GMP bound to VCA0042/PlzD, a PilZ domain-containing protein from Vibrio cholerae. Either this protein or another specific PilZ domain-containing protein is required for V. cholerae to efficiently infect mice. VCA0042/PlzD comprises a C-terminal PilZ domain plus an N-terminal domain with a similar beta-barrel fold. C-di-GMP contacts seven of the nine strongly conserved residues in the PilZ domain, including three in a seven-residue long N-terminal loop that undergoes a conformational switch as it wraps around c-di-GMP. This switch brings the PilZ domain into close apposition with the N-terminal domain, forming a new allosteric interaction surface that spans these domains and the c-di-GMP at their interface. The very small size of the N-terminal conformational switch is likely to explain the facile evolutionary diversification of the PilZ domain.
The structural basis of cyclic diguanylate signal transduction by PilZ domains., Benach J, Swaminathan SS, Tamayo R, Handelman SK, Folta-Stogniew E, Ramos JE, Forouhar F, Neely H, Seetharaman J, Camilli A, Hunt JF, EMBO J. 2007 Dec 12;26(24):5153-66. Epub 2007 Nov 22. PMID:18034161
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2rde is a 2 chain structure with sequence from Vibrio cholerae o395. Full crystallographic information is available from OCA.
See Also
Reference
- Benach J, Swaminathan SS, Tamayo R, Handelman SK, Folta-Stogniew E, Ramos JE, Forouhar F, Neely H, Seetharaman J, Camilli A, Hunt JF. The structural basis of cyclic diguanylate signal transduction by PilZ domains. EMBO J. 2007 Dec 12;26(24):5153-66. Epub 2007 Nov 22. PMID:18034161
Categories: Vibrio cholerae o395 | Benach, J. | Camilli, A. | Forouhar, F. | Handelman, S. | Hunt, J F. | NESG, Northeast Structural Genomics Consortium. | Neely, H. | Seetharaman, J. | Swaminathan, S S. | Tamayo, R. | C-di-gmp | Nesg | Northeast structural genomics consortium | Protein structure initiative | Psi-2 | Structural genomic | Unknown function | Vca0042 | Vibrio cholerae
