1l9l
From Proteopedia
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| - | [[Image:1l9l.jpg|left|200px]] | + | [[Image:1l9l.jpg|left|200px]] |
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| - | '''GRANULYSIN FROM HUMAN CYTOLYTIC T LYMPHOCYTES''' | + | {{Structure |
| + | |PDB= 1l9l |SIZE=350|CAPTION= <scene name='initialview01'>1l9l</scene>, resolution 0.92Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MPO:3[N-MORPHOLINO]PROPANE+SULFONIC+ACID'>MPO</scene> and <scene name='pdbligand=EOH:ETHANOL'>EOH</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''GRANULYSIN FROM HUMAN CYTOLYTIC T LYMPHOCYTES''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1L9L is a [ | + | 1L9L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L9L OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12488100 12488100] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: saposin fold]] | [[Category: saposin fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:28:24 2008'' |
Revision as of 10:28, 20 March 2008
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| , resolution 0.92Å | |||||||
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| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 20 12:28:24 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
