Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.6.1.1 extracted from

  • Qian, P.; Marklew, C.J.; Viney, J.; Davison, P.A.; Brindley, A.A.; Soederberg, C.; Al-Karadaghi, S.; Bullough, P.A.; Grossmann, J.G.; Hunter, C.N.
    Structure of the cyanobacterial Magnesium Chelatase H subunit determined by single particle reconstruction and small-angle X-ray scattering (2012), J. Biol. Chem., 287, 4946-4956.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Thermosynechococcus vestitus

Crystallization (Commentary)

Crystallization (Comment) Organism
using electron microscopy and small-angle x-ray scattering the structure of ChlH subunit is investigated. ChlH is a large, 148-kDa protein of 1326 residues, forming a cage-like assembly comprising the majority of the structure, attached to a globular N-terminal domain of 16 kDa by a narrow linker region. This N-terminal domain is adjacent to a 5 nm-diameter opening in the structure that allows access to a cavity Thermosynechococcus vestitus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
148000
-
-
Thermosynechococcus vestitus

Organism

Organism UniProt Comment Textmining
Thermosynechococcus vestitus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA chromatography Thermosynechococcus vestitus

Synonyms

Synonyms Comment Organism
chelatase H subunit
-
Thermosynechococcus vestitus
ChlH
-
Thermosynechococcus vestitus