| http://purl.uniprot.org/citations/22993092 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22993092 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22993092 | http://www.w3.org/2000/01/rdf-schema#comment | "Cyclic di-GMP (c-di-GMP) is a novel secondary-messenger molecule that is involved in regulating a plethora of important bacterial activities through binding to an unprecedented array of effectors. Proteins with a canonical PilZ domain that bind c-di-GMP play crucial roles in regulating flagellum-based motility. In contrast, noncanonical type II PilZ domains that do not effectively bind c-di-GMP regulate twitching motility, which is dependent on type IV pili (T4P). Recent data indicate that T4P biogenesis is initiated via the interaction of a noncanonical type II PilZ protein with the GGDEF/EAL-domain protein FimX and the pilus motor protein PilB at high c-di-GMP concentrations. However, the molecular details of such interactions remain to be elucidated. In this manuscript, the first hetero-complex crystal structure between a type II PilZ protein and the EAL domain of the FimX protein (FimX(EAL)) from Xanthomonas campestris pv. campestris (Xcc) in the presence of c-di-GMP is reported. This work reveals two novel conformations of monomeric c-di-GMP in the XccFimX(EAL)-c-di-GMP and XccFimX(EAL)-c-di-GMP-XccPilZ complexes, as well as a unique interaction mode of a type II PilZ domain with FimX(EAL). These findings indicate that c-di-GMP is sufficiently flexible to adjust its conformation to match the corresponding recognition motifs of different cognate effectors. Together, these results represent a first step towards an understanding of how T4P biogenesis is controlled by c-di-GMP at the molecular level and also of the ability of c-di-GMP to bind to a wide variety of effectors."xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.org/dc/terms/identifier | "doi:10.1107/S0907444912030594"xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.org/dc/terms/identifier | "doi:10.1107/s0907444912030594"xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/author | "Chou S.-H."xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/author | "Chou S.H."xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/author | "Yang M.T."xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/author | "Yang M.T."xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/author | "Chin K.H."xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/author | "Yu Y.-J."xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/author | "Liao Y.T."xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/author | "Yu Y.J."xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/author | "Chin K.-H."xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/author | "Kou W.-T."xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/author | "Liao Y.-T."xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/author | "Kuo W.T."xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/name | "Acta Crystallogr. D"xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/name | "Acta Crystallogr D Biol Crystallogr"xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/pages | "1380-1392"xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/pages | "1380-1392"xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/title | "Structural polymorphism of c-di-GMP bound to an EAL domain and in complex with a type II PilZ-domain protein."xsd:string |
| http://purl.uniprot.org/citations/22993092 | http://purl.uniprot.org/core/title | "Structural polymorphism of c-di-GMP bound to an EAL domain and in complex with a type II PilZ-domain protein."xsd:string |