3EIU
A second transient position of ATP on its trail to the nucleotide-binding site of subunit B of the motor protein A1Ao ATP synthase
Summary for 3EIU
| Entry DOI | 10.2210/pdb3eiu/pdb |
| Related | 2C61 2RKW 3B2Q 3DSR |
| Descriptor | V-type ATP synthase beta chain, ADENOSINE-5'-TRIPHOSPHATE, 4-(2-AMINOETHYL)BENZENESULFONYL FLUORIDE (3 entities in total) |
| Functional Keywords | hydrolase, atp synthesis, hydrogen ion transport, ion transport, transport |
| Biological source | Methanosarcina mazei (Methanosarcina frisia) |
| Total number of polymer chains | 2 |
| Total formula weight | 103877.79 |
| Authors | Manimekalai, S.M.S.,Kumar, A.,Balakrishna, A.M.,Gruber, G. (deposition date: 2008-09-17, release date: 2009-02-10, Last modification date: 2023-11-01) |
| Primary citation | Manimekalai, M.S.S.,Kumar, A.,Balakrishna, A.M.,Gruber, G. A second transient position of ATP on its trail to the nucleotide-binding site of subunit B of the motor protein A(1)A(O) ATP synthase J.Struct.Biol., 166:38-45, 2009 Cited by PubMed Abstract: The adenosine triphosphate (ATP) entrance into the nucleotide-binding subunits of ATP synthases is a puzzle. In the previously determined structure of subunit B mutant R416W of the Methanosarcina mazei Gö1 A-ATP synthase one ATP could be trapped at a transition position, close to the phosphate-binding loop. Using defined parameters for co-crystallization of an ATP-bound B-subunit, a unique transition position of ATP could be found in the crystallographic structure of this complex, solved at 3.4 A resolution. The nucleotide is found near the helix-turn-helix motif in the C-terminal domain of the protein; the location occupied by the gamma-subunit to interact with the empty beta-subunit in the thermoalkaliphilic Bacillus sp. TA2.A1 of the related F-ATP synthase. When compared with the determined structure of the ATP-transition position, close to the P-loop, and the nucleotide-free form of subunit B, the C-terminal domain of the B mutant is rotated by around 6 degrees, implicating an ATP moving pathway. We propose that, in the nucleotide empty state the central stalk subunit D is in close contact with subunit B and when the ATP molecule enters, D moves slightly, paving way for it to interact with the subunit B, which makes the C-terminal domain rotate by 6 degrees. PubMed: 19138746DOI: 10.1016/j.jsb.2008.12.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.43 Å) |
Structure validation
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