Cloned (Comment) | Organism |
---|---|
gene ndhS , recombinant expression of two NDH-1L subunits, NdhS and ferredoxin | Thermosynechococcus vestitus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | preparation of NDH-Fd supercomplex: the purified NDH-1L complex is concentrated to 1 mg/ml and mixed with NdhS, NdhV, and Fd proteins. The molar ratio of NDH-1L:NdhS:NdhV:Fd is set to 1:4:6:6. The mixture is incubated for 1 h at 20°C and then concentrated to 12 mg/ml | Thermosynechococcus vestitus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
thylakoid membrane | the NDH-1L is more rigid in the membrane arm at low pH, whereas the complex is more strongly associated between its two arms at higher pH | Thermosynechococcus vestitus | 42651 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | bound in [4Fe-4S] clusters and ferredoxin | Thermosynechococcus vestitus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | Thermosynechococcus vestitus | - |
2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermosynechococcus vestitus | Q8DKZ3 | - |
- |
Purification (Comment) | Organism |
---|---|
native NDH-1L complex from strain BP-1 by membrane preparation through ultracentrifugation at 150000 x g, nickel affinity chromatography (owing to the native histidine-rich area within the hydrophobic subunit NdhF1), and solubilization with 1% w/v n-dodecyl-beta-D-maltoside, followed by again nickel affinity chromatography, ultrafiltration, and gel filtration | Thermosynechococcus vestitus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | - |
Thermosynechococcus vestitus | 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | analysis of binding manner of NDH-1L with Fd and PQ, binding structures, overview | Thermosynechococcus vestitus | 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
additional information | the ferredoxin (Fd) binding pocket is mainly formed by subunits NdhI and NdhH, structure overview. Fd and NdhV almost symmetrically bind the hairpin loop of NdhI from the opposite sides | Thermosynechococcus vestitus | ? | - |
- |
Subunits | Comment | Organism |
---|---|---|
More | two structures of NDH-1L from Thermosynechococcus elongatus strain BP-1, in complex with one ferredoxin (Fd) and an endogenous plastoquinone (PQ), respectively. Comparison of NDH-PQ structure (NDHpH7) with previously reported two NDH-1L structures NDHpH6 and NDHpH8 (PDB IDs 6NBY and 6HUM) superposed on NdhA subunit, overview | Thermosynechococcus vestitus |
Synonyms | Comment | Organism |
---|---|---|
NAD(P)H dehydrogenase-like (NDH) complex | - |
Thermosynechococcus vestitus |
NDH-1L | - |
Thermosynechococcus vestitus |
NdhL | - |
Thermosynechococcus vestitus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Thermosynechococcus vestitus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | 8 | - |
Thermosynechococcus vestitus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
comparison of NDH-PQ structure (NDHpH7) with previously reported two NDH-1L structures NDHpH6 and NDHpH8 (PDB IDs 6NBY and 6HUM) superposed on NdhA subunit, overview | Thermosynechococcus vestitus |
6 | 9 | highly reduced activity at pH 6.0 and pH 9.0, maximal activity at pH 7.0-8.0 | Thermosynechococcus vestitus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
Ferredoxin | - |
Thermosynechococcus vestitus | |
plastoquinone | - |
Thermosynechococcus vestitus | |
[4Fe-4S] cluster | - |
Thermosynechococcus vestitus |
General Information | Comment | Organism |
---|---|---|
additional information | NDH-1L structure modeling, structure-function analysis, overview. Analysis of the binding manner of NDH-1L with Fd and PQ, as well as the structural elements crucial for proper functioning of the NDH-1L complex. The hydrophilic arm contains nine NDH subunits, including NdhV and the [4Fe-4S] clusters, the NDH-1L is more rigid in the membrane arm at low pH, whereas the complex is more strongly associated between its two arms at higher pH. NdhV is composed of central loops/beta-strands, which is flanked by the N- and C-terminal helix at one side. In the NDH-Fd structure, NdhV is located above NdhN and NdhS. The central loops/beta-strands of NdhV join with the loops/beta-strands of NdhS, forming strong interactions. In NDH complex, the soluble subunits NdhK and NdhH together with the membrane subunit NdhA play major role in maintaining the association between the membrane and hydrophilic arms. In addition, NdhI, NdhC, and the OPS subunit NdhL also contribute to the interaction between the two arms. The cytoplasmic loop between the first and second TMH (TMH1-2 loop) of NdhC contacts NdhA and the soluble subunits NdhK/NdhH/NdhM, reinforcing the interactions between the two arms. Moreover, the membrane subunit NdhL has a C-terminal fragment projecting into the cytoplasmic region and associating with NdhI/NdhN. While the soluble NdhI possesses an N-terminal amphiphilic helix (N-helix) that embraces the membrane subunits NdhA/NdhL. In addition, three lipid molecules are found at the interface between the two arms, facilitating their association. Two of these lipids link the N-helix of NdhI with the membrane domain of NdhA and NdhC, whereas the third lipid is located in an enclosed cavity formed by the N-terminal fragments from NdhL, NdhN, and NdhK. Pivotal role of lipid molecules in connecting the hydrophilic arm with the membrane arm of the NDH complex | Thermosynechococcus vestitus |
physiological function | NAD(P)H dehydrogenase-like (NDH) complex NDH-1L of cyanobacteria plays a crucial role in cyclic electron flow (CEF) around photosystem I and respiration processes. NDH-1L couples the electron transport from ferredoxin (Fd) to plastoquinone (PQ) and proton pumping from cytoplasm to the lumen that drives the ATP production. NDH-1L-dependent CEF increases the ATP/NADPH ratio, and is therefore pivotal for oxygenic phototrophs to function under stress | Thermosynechococcus vestitus |