1vfj: Difference between revisions

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{{STRUCTURE_1vfj|  PDB=1vfj  |  SCENE=  }}  
{{STRUCTURE_1vfj|  PDB=1vfj  |  SCENE=  }}  


'''Crystal structure of TT1020 from Thermus thermophilus HB8'''
===Crystal structure of TT1020 from Thermus thermophilus HB8===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Signal transducing protein]]
[[Category: Signal transducing protein]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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