PDBsum entry 4u02

Transport protein

PDB id: 4u02

Contents

Protein chains

243 a.a.

Ligands

SO4 ×4

Waters ×304

PDB id:

4u02

Name:

Transport protein

Title:

Crystal structure of apo-ttha1159

Structure:

Amino acid abc transporter, atp-binding protein. Chain: a, b, c, d. Engineered: yes

Source:

Thermus thermophilus hb8. Organism_taxid: 300852. Gene: ttha1159. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.40Å R-factor: 0.204 R-free: 0.250

Authors:

S.Karthiga Devi,V.P.R.Chichili,D.Velmurugan,J.Sivaraman

Key ref:

S.K.Devi et al. (2015). Structural basis for the hydrolysis of ATP by a nucleotide binding subunit of an amino acid ABC transporter from Thermus thermophilus. J Struct Biol, 190, 367-372. PubMed id: 25916755 DOI: 10.1016/j.jsb.2015.04.012

Date:

11-Jul-14 Release date: 13-May-15

Protein chains

Q5SJ55  (Q5SJ55_THET8) -  Amino acid ABC transporter, ATP-binding protein from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

Seq: 244 a.a.

Struc: 243 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.jsb.2015.04.012

J Struct Biol 190:367-372 (2015)

PubMed id: 25916755

Structural basis for the hydrolysis of ATP by a nucleotide binding subunit of an amino acid ABC transporter from Thermus thermophilus.

S.K.Devi, V.P.Chichili, J.Jeyakanthan, D.Velmurugan, J.Sivaraman.

ABSTRACT

ATP-binding cassette (ABC) transporters are a major family of small molecule transporter proteins, and their deregulation is associated with several diseases, including cancer. Here, we report the crystal structure of the nucleotide binding domain (NBD) of an amino acid ABC transporter from Thermus thermophilus (TTHA1159) in its apo form and as a complex with ADP along with functional studies. TTHA1159 is a putative arginine ABC transporter. The apo-TTHA1159 was crystallized in dimeric form, a hitherto unreported form of an apo NBD. Structural comparison of the apo and ADP-Mg(2+) complexes revealed that Phe14 of TTHA1159 undergoes a significant conformational change to accommodate ADP, and that the bound ADP interacts with the P-loop (Gly40-Thr45). Modeling of ATP-Mg(2+):TTHA1159 complex revealed that Gln86 and Glu164 are involved in water-mediated hydrogen bonding contacts and Asp163 in Mg(2+) ion-mediated hydrogen bonding contacts with the γ-phosphate of ATP, consistent with the findings of other ABC transporters. Mutational studies confirmed the necessity of each of these residues, and a comparison of the apo/ADP Mg(2+):TTHA1159 with its ATP-complex model suggests the likelihood of a key conformational change to the Gln86 side chain for ATP hydrolysis.