4U02

Crystal structure of apo-TTHA1159

Summary for 4U02

• Entry DOI: 10.2210/pdb4u02/pdb
• Related: 4U00
• Descriptor: Amino acid ABC transporter, ATP-binding protein, SULFATE ION (3 entities in total)
• Functional Keywords: atp binding protein, abc amino acid transporter, nucleotide binding domain, transport protein
• Biological source: Thermus thermophilus HB8
• Total number of polymer chains: 4
• Total formula weight: 111705.92

Authors

Karthiga Devi, S.,Chichili, V.P.R.,Velmurugan, D.,Sivaraman, J. (deposition date: 2014-07-11, release date: 2015-05-13, Last modification date: 2024-03-20)

Primary citation

Devi, S.K.,Chichili, V.P.,Jeyakanthan, J.,Velmurugan, D.,Sivaraman, J.
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, 2015

PubMed 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.

PubMed: 25916755
DOI: 10.1016/j.jsb.2015.04.012

Experimental method

X-RAY DIFFRACTION (2.399 Å)