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http://purl.uniprot.org/citations/15629661http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15629661http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15629661http://www.w3.org/2000/01/rdf-schema#comment"The Thermus thermophilus HB8 genome encodes a signal transducing PII protein, GlnK. The crystal structures of GlnK have been determined in two different space groups, P2(1)2(1)2(1) and P3(1)21. The PII protein has the T-loop, which is essential for interactions with receptor proteins. In both crystal forms, three GlnK molecules form a trimer in the asymmetric unit. In one P2(1)2(1)2(1) crystal form, the three T-loops in the trimer are disordered, while in another P2(1)2(1)2(1) crystal form, the T-loop from one molecule in the trimer is ordered. In the P3(1)21 crystal, one T-loop is ordered while the other two T-loops are disordered. The conformations of the ordered T-loops significantly differ between the two crystal forms; one makes the alpha-helix in the middle of the T-loop, while the other has an extension of the beta-hairpin. Two different conformations are captured by the crystal contacts. The observation of multiple T-loop conformations suggests that the T-loop could potentially exhibit "polysterism," which would be important for interactions with receptor proteins. The crystal structures of the nucleotide-bound forms, GlnK.ATP and GlnK.ADP, have also been determined. ATP/ADP binding within a cleft at the interface of two adjacent T. thermophilus GlnK monomers might affect the conformation of the T-loop."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.org/dc/terms/identifier"doi:10.1016/j.jsb.2004.08.007"xsd:string
http://purl.uniprot.org/citations/15629661http://purl.org/dc/terms/identifier"doi:10.1016/j.jsb.2004.08.007"xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Kuramitsu S."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Kuramitsu S."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Shirouzu M."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Shirouzu M."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Sakai H."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Sakai H."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Terada T."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Terada T."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Yokoyama S."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Yokoyama S."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Wang H."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Wang H."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Yamaguchi H."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Yamaguchi H."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Kaminishi T."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Kaminishi T."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Takemoto-Hori C."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Takemoto-Hori C."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Kamewari Y."xsd:string
http://purl.uniprot.org/citations/15629661http://purl.uniprot.org/core/author"Kamewari Y."xsd:string