3PCV: Crystal Structure Analysis Of Human Leukotriene C4 Synthase At 1.9 Angstrom Resolution

Citation:
Abstract
Leukotriene (LT) C(4) and its metabolites, LTD(4) and LTE(4), are involved in the pathobiology of bronchial asthma. LTC(4) synthase is the nuclear membrane-embedded enzyme responsible for LTC(4) biosynthesis, catalyzing the conjugation of two substrates that have considerably different water solubility; that amphipathic LTA(4) as a derivative of arachidonic acid and a water-soluble glutathione (GSH). A previous crystal structure revealed important details of GSH binding and implied a GSH activating function for Arg-104. In addition, Arg-31 was also proposed to participate in the catalysis based on the putative LTA(4) binding model. In this study enzymatic assay with mutant enzymes demonstrates that Arg-104 is required for the binding and activation of GSH and that Arg-31 is needed for catalysis probably by activating the epoxide group of LTA(4).
PDB ID: 3PCVDownload
MMDB ID: 89242
PDB Deposition Date: 2010/10/22
Updated in MMDB: 2011/12
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 3PCV: trimeric; determined by author and by software (PISA)
Molecular Components in 3PCV
Label Count Molecule
Proteins (3 molecules)
3
Leukotriene C4 Synthase(Gene symbol: LTC4S)
Molecule annotation
Chemicals (51 molecules)
1
3
2
27
3
12
4
3
5
6
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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