- PDB-2rq7: Solution structure of the epsilon subunit chimera combining the N... -
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Basic information
Entry
Database: PDB / ID: 2rq7
Title
Solution structure of the epsilon subunit chimera combining the N-terminal beta-sandwich domain from T. Elongatus bp-1 f1 and the C-terminal alpha-helical domain from spinach chloroplast F1
Components
ATP synthase epsilon chain,ATP synthase epsilon chain, chloroplastic
Keywords
HYDROLASE / ATP SYNTHASE / F1FO ATP SYNTHASE / F1-ATPASE / EPSILON SUBUNIT / CHLOROPLAST / ATP SYNTHESIS / CF1 / HYDROGEN ION TRANSPORT / ION TRANSPORT / MEMBRANE / THYLAKOID / TRANSPORT / PLASTID / CF(1)
Function / homology
Function and homology information
plasma membrane-derived thylakoid membrane / proton motive force-driven ATP synthesis / chloroplast thylakoid membrane / proton-transporting ATP synthase complex, catalytic core F(1) / proton-transporting ATP synthase activity, rotational mechanism / ATP binding Similarity search - Function
Helix Hairpins - #480 / ATP Synthase; domain 1 / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase delta/epsilon subunit, C-terminal domain / ATP synthase, Delta/Epsilon chain, long alpha-helix domain / Helix Hairpins / ATP synthase, F1 complex, delta/epsilon subunit / ATP synthase, F1 complex, delta/epsilon subunit, N-terminal / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, Delta/Epsilon chain, beta-sandwich domain ...Helix Hairpins - #480 / ATP Synthase; domain 1 / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase delta/epsilon subunit, C-terminal domain / ATP synthase, Delta/Epsilon chain, long alpha-helix domain / Helix Hairpins / ATP synthase, F1 complex, delta/epsilon subunit / ATP synthase, F1 complex, delta/epsilon subunit, N-terminal / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, Delta/Epsilon chain, beta-sandwich domain / Helix non-globular / Special / Sandwich / Mainly Beta Similarity search - Domain/homology
ATPsynthaseepsilonchain,ATPsynthaseepsilonchain, chloroplastic / ATP synthase F1 sector epsilon subunit / F-ATPase epsilon subunit
Mass: 14602.535 Da / Num. of mol.: 1 / Mutation: K109A Source method: isolated from a genetically manipulated source Details: The fusion protein of beta-sandwich domain (residues 1-88) from T. Elongatus bp-1 F1 and alpha-helical domain (residues 89-134) from spinach chloroplast F1 Source: (gene. exp.) Thermosynechococcus elongatus (strain BP-1) (bacteria), (gene. exp.) Spinacia oleracea (spinach) Strain: BP-1 / Gene: atpC, atpE, tlr0526, atpE / Production host: Escherichia coli (E. coli) / References: UniProt: Q8DLG7, UniProt: P00833
Sequence details
THE FUSION PROTEIN OF BETA-SANDWICH DOMAIN (RESIDUES 1-88) FROM T. ELONGATUS BP-1 F1 AND ALPHA- ...THE FUSION PROTEIN OF BETA-SANDWICH DOMAIN (RESIDUES 1-88) FROM T. ELONGATUS BP-1 F1 AND ALPHA-HELICAL DOMAIN (RESIDUES 89-134) FROM SPINACH CHLOROPLAST F1
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
2D 1H-15N HSQC
1
2
1
3D HN(CA)CB
1
3
1
3DCBCA(CO)NH
1
4
1
2D 1H-1H NOESY
1
5
1
3DH(CCO)NH
1
6
1
3D 1H-15N NOESY
1
7
1
3D 1H-13C NOESY
1
8
1
3DHBHA(CO)NH
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Sample preparation
Details
Contents: 1.0 mM [U-99% 15N] ATP SYNTHASE EPSILON CHAIN-1, 1.0 mM [U-99% 13C; U-99% 15N] ATP SYNTHASE EPSILON CHAIN-2, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O
Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1
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