4cbj | pdb_00004cbj

The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology

spinqualitylabelsall models 4cbj, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cbj is a 13 chain structure with sequence from Alkalihalophilus pseudofirmus OF4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: DPV, FME, LMT, TAM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ATPL_ALKPO F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.[HAMAP-Rule:MF_01396] Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396] Publication Abstract from PubMed In the c-ring rotor of ATP synthases ions are shuttled across the membrane during ATP synthesis by a unique rotary mechanism. We investigated characteristics of the c-ring from the alkaliphile Bacillus pseudofirmus OF4 with respect to evolutionary adaptations to operate with protons at high environmental pH. The X-ray structures of the wild-type c13 ring at pH 9.0 and a 'neutralophile-like' mutant (P51A) at pH 4.4, at 2.4 and 2.8 A resolution, respectively, reveal a dependency of the conformation and protonation state of the proton-binding glutamate (E54 ) on environmental hydrophobicity. Faster labeling kinetics with the inhibitor dicyclohexylcarbodiimide (DCCD) demonstrate a greater flexibility of E54 in the mutant due to reduced water occupancy within the H+ -binding site. A second 'neutralophile-like' mutant (V21N) shows reduced growth at high pH, which is explained by restricted conformational freedom of the mutant's E54 carboxylate. The study directly connects subtle structural adaptations of the c-ring ion-binding site to in vivo effects of alkaliphile cell physiology. The c-ring ion-binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle.,Preiss L, Langer JD, Hicks DB, Liu J, Yildiz O, Krulwich TA, Meier T Mol Microbiol. 2014 Apr 8. doi: 10.1111/mmi.12605. PMID:24707994 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase 3D structures

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