PDBsum entry 1v3s

Signaling protein

PDB id: 1v3s

Contents

Protein chains

97 a.a. *

91 a.a. *

Ligands

ATP ×3

Waters ×153

* Residue conservation analysis

PDB id:

1v3s

Name:

Signaling protein

Title:

Crystal structure of tt1020 from thermus thermophilus hb8

Structure:

Nitrogen regulatory protein p-ii. Chain: a, b, c. Engineered: yes. Mutation: yes

Source:

Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Trimer (from PQS)

Resolution:

1.85Å R-factor: 0.201 R-free: 0.243

Authors:

H.Wang,H.Sakai,C.Takemoto-Hori,T.Kaminishi,T.Terada,S.Kuramitsu, M.Shirouzu,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

H.Sakai et al. (2005). Crystal structures of the signal transducing protein GlnK from Thermus thermophilus HB8. J Struct Biol, 149, 99. PubMed id: 15629661 DOI: 10.1016/j.jsb.2004.08.007

Date:

05-Nov-03 Release date: 23-Nov-04

Protein chains

P83820  (P83820_THETH) -  Signaling protein from Thermus thermophilus

Seq: 116 a.a.

Struc: 97 a.a.

Protein chain

P83820  (P83820_THETH) -  Signaling protein from Thermus thermophilus

Seq: 116 a.a.

Struc: 91 a.a.

DOI no: 10.1016/j.jsb.2004.08.007

J Struct Biol 149:99 (2005)

PubMed id: 15629661

Crystal structures of the signal transducing protein GlnK from Thermus thermophilus HB8.

H.Sakai, H.Wang, C.Takemoto-Hori, T.Kaminishi, H.Yamaguchi, Y.Kamewari, T.Terada, S.Kuramitsu, M.Shirouzu, S.Yokoyama.

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.