2hky
From Proteopedia
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'''NMR solution structure of human RNase 7'''<br /> | '''NMR solution structure of human RNase 7'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2HKY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2HKY is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: rnase]] | [[Category: rnase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:32:39 2008'' |
Revision as of 15:32, 15 February 2008
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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
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