3B29

Human leukotriene C4 synthase in complex with dodecyl-beta-D-selenomaltoside

Summary for 3B29

• Entry DOI: 10.2210/pdb3b29/pdb
• Related: 2PNO 3PCV
• Descriptor: Leukotriene C4 synthase, GLUTATHIONE, SULFATE ION, ... (5 entities in total)
• Functional Keywords: membrane protein, helix bundle, homo trimer, mgst, mapeg, lyase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus outer membrane; Multi-pass membrane protein: Q16873
• Total number of polymer chains: 1
• Total formula weight: 20682.81

Authors

Saino, H.,Ago, H.,Miyano, M. (deposition date: 2011-07-22, release date: 2011-12-14, Last modification date: 2024-03-13)

Primary citation

Saino, H.,Ago, H.,Ukita, Y.,Miyano, M.
Seleno-detergent MAD phasing of leukotriene C4 synthase in complex with dodecyl-beta-D-selenomaltoside
Acta Crystallogr.,Sect.F, 67:1666-1673, 2011

PubMed Abstract: Dodecyl-β-D-selenomaltoside (SeDDM) is a seleno-detergent with a β-glycosidic seleno-ether in place of the ether moiety in dodecyl-β-D-maltoside. Seleno-detergents are candidates for heavy-atom agents in experimental phasing of membrane proteins in protein crystallography. Crystals of a nuclear membrane-embedded enzyme, leukotriene C(4) synthase (LTC(4)S), in complex with SeDDM were prepared and a multiwavelength anomalous diffraction (MAD) experiment was performed. The SeDDM in the LTC(4)S crystal exhibited sufficient anomalous diffraction for determination of the structure using MAD phasing.

PubMed: 22139193
DOI: 10.1107/S1744309111042345

Experimental method

X-RAY DIFFRACTION (3.2 Å)