1V3S

Crystal structure of TT1020 from Thermus thermophilus HB8

Summary for 1V3S

• Entry DOI: 10.2210/pdb1v3s/pdb
• Related: 1V3R
• Descriptor: Nitrogen regulatory protein P-II, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: structural genomics, signal transducing protein, riken structural genomics/proteomics initiative, rsgi, nppsfa, national project on protein structural and functional analyses, signaling protein
• Biological source: Thermus thermophilus
• Total number of polymer chains: 3
• Total formula weight: 40224.47

Authors

Wang, H.,Sakai, H.,Takemoto-Hori, C.,Kaminishi, T.,Terada, T.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-11-05, release date: 2004-11-23, Last modification date: 2023-12-27)

Primary citation

Sakai, H.,Wang, H.,Takemoto-Hori, C.,Kaminishi, T.,Yamaguchi, H.,Kamewari, Y.,Terada, T.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.
Crystal structures of the signal transducing protein GlnK from Thermus thermophilus HB8.
J.Struct.Biol., 149:99-110, 2005

PubMed Abstract: 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.

PubMed: 15629661
DOI: 10.1016/j.jsb.2004.08.007

Experimental method

X-RAY DIFFRACTION (1.85 Å)