2hky
From Proteopedia
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| - | [[Image:2hky.jpg|left|200px]] | + | [[Image:2hky.jpg|left|200px]] |
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| - | '''NMR solution structure of human RNase 7''' | + | {{Structure |
| + | |PDB= 2hky |SIZE=350|CAPTION= <scene name='initialview01'>2hky</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= RNASE7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''NMR solution structure of human RNase 7''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2HKY is a [ | + | 2HKY 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=2HKY OCA]. |
==Reference== | ==Reference== | ||
| - | The flexible and clustered lysine residues of human ribonuclease 7 are critical for membrane permeability and antimicrobial activity., Huang YC, Lin YM, Chang TW, Wu SJ, Lee YS, Chang MD, Chen C, Wu SH, Liao YD, J Biol Chem. 2007 Feb 16;282(7):4626-33. Epub 2006 Dec 6. PMID:[http:// | + | The flexible and clustered lysine residues of human ribonuclease 7 are critical for membrane permeability and antimicrobial activity., Huang YC, Lin YM, Chang TW, Wu SJ, Lee YS, Chang MD, Chen C, Wu SH, Liao YD, J Biol Chem. 2007 Feb 16;282(7):4626-33. Epub 2006 Dec 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17150966 17150966] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rnase]] | [[Category: rnase]] | ||
| - | ''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 17:18:26 2008'' |
Revision as of 15:18, 20 March 2008
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| Gene: | RNASE7 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR solution structure of human RNase 7
Overview
The ubiquitous ribonucleases (RNases) play important roles in RNA metabolism, angiogenesis, neurotoxicity, and antitumor or antimicrobial activity. Only the antimicrobial RNases possess high positively charged residues, although their mechanisms of action remain unclear. Here, we report on the role of cationic residues of human RNase7 (hRNase7) in its antimicrobial activity. It exerted antimicrobial activity against bacteria and yeast, even at 4 degrees C. The bacterial membrane became permeable to the DNA-binding dye SYTOX(R) Green in only a few minutes after bactericidal RNase treatment. NMR studies showed that the 22 positively charged residues (Lys(18) and Arg(4)) are distributed into three clusters on the surface of hRNase7. The first cluster, K(1),K(3),K(111),K(112), was located at the flexible coil near the N terminus, whereas the other two, K(32),K(35) and K(96),R(97),K(100), were located on rigid secondary structures. Mutagenesis studies showed that the flexible cluster K(1),K(3),K(111),K(112), rather than the catalytic residues His(15), Lys(38), and His(123) or other clusters such as K(32),K(35) and K(96),R(97),K(100), is critical for the bactericidal activity. We suggest that the hRNase7 binds to bacterial membrane and renders the membrane permeable through the flexible and clustered Lys residues K(1),K(3),K(111),K(112). The conformation of hRNase7 can be adapted for pore formation or disruption of bacterial membrane even at 4 degrees C.
About this Structure
2HKY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The flexible and clustered lysine residues of human ribonuclease 7 are critical for membrane permeability and antimicrobial activity., Huang YC, Lin YM, Chang TW, Wu SJ, Lee YS, Chang MD, Chen C, Wu SH, Liao YD, J Biol Chem. 2007 Feb 16;282(7):4626-33. Epub 2006 Dec 6. PMID:17150966
Page seeded by OCA on Thu Mar 20 17:18:26 2008
