PDBsum entry 2pmh

Transcription regulator

PDB id: 2pmh

Contents

Protein chain

150 a.a. *

Ligands

GLN

Metals

_MG

_NA ×3

Waters ×64

* Residue conservation analysis

PDB id:

2pmh

Name:

Transcription regulator

Title:

Crystal structure of thr132ala of st1022 from sulfolobus tokodaii

Structure:

150aa long hypothetical transcriptional regulator. Chain: a. Synonym: st1022. Engineered: yes. Mutation: yes

Source:

Sulfolobus tokodaii. Organism_taxid: 273063. Strain: 7. Gene: st1022. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.90Å R-factor: 0.242 R-free: 0.244

Authors:

T.S.Kumarevel,P.Karthe,N.Nakano,A.Shinkai,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

T.Kumarevel et al. (2008). Crystal structure of glutamine receptor protein from Sulfolobus tokodaii strain 7 in complex with its effector L-glutamine: implications of effector binding in molecular association and DNA binding. Nucleic Acids Res, 36, 4808-4820. PubMed id: 18653535

Date:

22-Apr-07 Release date: 22-Apr-08

Protein chain

F9VNT4  (F9VNT4_SULTO) -  Glutamine receptor protein from Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)

Seq: 150 a.a.

Struc: 150 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

Nucleic Acids Res 36:4808-4820 (2008)

PubMed id: 18653535

Crystal structure of glutamine receptor protein from Sulfolobus tokodaii strain 7 in complex with its effector L-glutamine: implications of effector binding in molecular association and DNA binding.

T.Kumarevel, N.Nakano, K.Ponnuraj, S.C.Gopinath, K.Sakamoto, A.Shinkai, P.K.Kumar, S.Yokoyama.

ABSTRACT

Genome analyses have revealed that members of the Lrp/AsnC family of transcriptional regulators are widely distributed among prokaryotes, including both bacteria and archaea. These regulatory proteins are involved in cellular metabolism in both global and specific manners, depending on the availability of the exogenous amino acid effectors. Here we report the first crystal structure of glutamine receptor protein (Grp) from Sulfolobus tokodaii strain 7, in the ligand-free and glutamine-bound (Grp-Gln) forms. Although the overall structures of both molecules are similar, a significant conformational change was observed at the ligand [L-glutamine (Gln)] binding site in the effector domain, which may be essential for further stabilization of the octameric structure, and in turn for facilitating DNA binding. In addition, we predicted promoter for the grp gene, and these analyses suggested the importance of cooperative binding to the protein. To gain insights into the ligand-induced conformational changes, we mutated all of the ligand-binding residues in Grp, and revealed the importance of Gln binding by biochemical and structural analyses. Further structural analyses showed that Y77 is crucial for ligand binding, and that the residues T132 and T134, which are highly conserved among the Lrp family of proteins, fluctuates between the active and inactive conformations, thus affecting protein oligomerization for DNA binding.