1l9l
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Our crystal structure of granulysin suggests a mechanism for lysis of | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Anderson, D | + | [[Category: Anderson, D H.]] |
[[Category: Cascio, D.]] | [[Category: Cascio, D.]] | ||
[[Category: Eisenberg, D.]] | [[Category: Eisenberg, D.]] | ||
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[[Category: Krensky, A.]] | [[Category: Krensky, A.]] | ||
[[Category: Modlin, R.]] | [[Category: Modlin, R.]] | ||
| - | [[Category: Sawaya, M | + | [[Category: Sawaya, M R.]] |
[[Category: EOH]] | [[Category: EOH]] | ||
[[Category: MPO]] | [[Category: MPO]] | ||
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[[Category: saposin fold]] | [[Category: saposin fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:48 2008'' |
Revision as of 11:42, 21 February 2008
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GRANULYSIN FROM HUMAN CYTOLYTIC T LYMPHOCYTES
Overview
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.
About this Structure
1L9L is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
Granulysin crystal structure and a structure-derived lytic mechanism., Anderson DH, Sawaya MR, Cascio D, Ernst W, Modlin R, Krensky A, Eisenberg D, J Mol Biol. 2003 Jan 10;325(2):355-65. PMID:12488100
Page seeded by OCA on Thu Feb 21 13:42:48 2008
Categories: Homo sapiens | Single protein | Anderson, D H. | Cascio, D. | Eisenberg, D. | Ernst, W. | Krensky, A. | Modlin, R. | Sawaya, M R. | EOH | MPO | SO4 | Granulysin | Membrane-lytic | Saposin fold
