1L9L

GRANULYSIN FROM HUMAN CYTOLYTIC T LYMPHOCYTES

Summary for 1L9L

• Entry DOI: 10.2210/pdb1l9l/pdb
• Descriptor: Granulysin, SULFATE ION, 3[N-MORPHOLINO]PROPANE SULFONIC ACID, ... (5 entities in total)
• Functional Keywords: granulysin, saposin fold, membrane-lytic, antimicrobial protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P22749
• Total number of polymer chains: 1
• Total formula weight: 9410.81

Authors

Anderson, D.H.,Sawaya, M.R.,Cascio, D.,Ernst, W.,Krensky, A.,Modlin, R.,Eisenberg, D. (deposition date: 2002-03-25, release date: 2002-11-06, Last modification date: 2024-11-06)

Primary citation

Anderson, D.H.,Sawaya, M.R.,Cascio, D.,Ernst, W.,Modlin, R.,Krensky, A.,Eisenberg, D.
Granulysin Crystal Structure and a Structure-Derived Lytic Mechanism
J.Mol.Biol., 325:355-365, 2002

PubMed Abstract: Our crystal structure of granulysin suggests a mechanism for lysis of bacterial membranes by granulysin, a 74-residue basic protein from human cytolytic T lymphocyte and natural killer cells. We determined the initial crystal structure of selenomethionyl granulysin by MAD phasing at 2A resolution. We present the structure model refined using native diffraction data to 0.96A resolution. The five-helical bundle of granulysin resembles other "saposin folds" (such as NK-lysin). Positive charges distribute in a ring around the granulysin molecule, and one face has net positive charge. Sulfate ions bind near the segment of the molecule identified as most membrane-lytic and of highest hydrophobic moment. The ion locations may indicate granulysin's orientation of initial approach towards the membrane. The crystal packing reveals one way to pack a sheet of granulysin molecules at the cell surface for a concerted lysis effort. The energy of binding granulysin charges to the bacterial membrane could drive the subsequent lytic processes. The loosely packed core facilitates a hinge or scissors motion towards exposure of hydrophobic surface that we propose tunnels the granulysin into the fracturing target membrane.

PubMed: 12488100
DOI: 10.1016/S0022-2836(02)01234-2

Experimental method

X-RAY DIFFRACTION (0.92 Å)