1m07: Difference between revisions

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New page: left|200px<br /><applet load="1m07" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m07, resolution 1.80Å" /> '''RESIDUES INVOLVED IN...
 
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[[Image:1m07.gif|left|200px]]<br /><applet load="1m07" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1m07.gif|left|200px]]<br /><applet load="1m07" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1m07, resolution 1.80&Aring;" />
caption="1m07, resolution 1.80&Aring;" />
'''RESIDUES INVOLVED IN THE CATALYSIS AND BASE SPECIFICITY OF CYTOTOXIC RIBONUCLEASE FROM BULLFROG (RANA CATESBEIANA)'''<br />
'''RESIDUES INVOLVED IN THE CATALYSIS AND BASE SPECIFICITY OF CYTOTOXIC RIBONUCLEASE FROM BULLFROG (RANA CATESBEIANA)'''<br />


==Overview==
==Overview==
The Rana catesbeiana (bullfrog) ribonucleases, which belong to the RNase A, superfamily, exert cytotoxicity toward tumor cells. RC-RNase, the most, active among frog ribonucleases, has a unique base preference for, pyrimidine-guanine rather than pyrimidine-adenine in RNase A. Residues of, RC-RNase involved in base specificity and catalytic activity were, determined by site-directed mutagenesis, k(cat)/K(m) analysis toward, dinucleotides, and cleavage site analysis of RNA substrate. The results, show that Pyr-1 (N-terminal pyroglutamate), Lys-9, and Asn-38 along with, His-10, Lys-35, and His-103 are involved in catalytic activity, whereas, Pyr-1, Thr-39, Thr-70, Lys-95, and Glu-97 are involved in base, specificity. The cytotoxicity of RC-RNase is correlated, but not, proportional to, its catalytic activity. The crystal structure of the, RC-RNase.d(ACGA) complex was determined at 1.80 A resolution. Residues, Lys-9, His-10, Lys-35, and His-103 interacted directly with catalytic, phosphate at the P(1) site, and Lys-9 was stabilized by hydrogen bonds, contributed by Pyr-1, Tyr-28, and Asn-38. Thr-70 acts as a hydrogen bond, donor for cytosine through Thr-39 and determines B(1) base specificity., Interestingly, Pyr-1 along with Lys-95 and Glu-97 form four hydrogen bonds, with guanine at B(2) site and determine B(2) base specificity.
The Rana catesbeiana (bullfrog) ribonucleases, which belong to the RNase A superfamily, exert cytotoxicity toward tumor cells. RC-RNase, the most active among frog ribonucleases, has a unique base preference for pyrimidine-guanine rather than pyrimidine-adenine in RNase A. Residues of RC-RNase involved in base specificity and catalytic activity were determined by site-directed mutagenesis, k(cat)/K(m) analysis toward dinucleotides, and cleavage site analysis of RNA substrate. The results show that Pyr-1 (N-terminal pyroglutamate), Lys-9, and Asn-38 along with His-10, Lys-35, and His-103 are involved in catalytic activity, whereas Pyr-1, Thr-39, Thr-70, Lys-95, and Glu-97 are involved in base specificity. The cytotoxicity of RC-RNase is correlated, but not proportional to, its catalytic activity. The crystal structure of the RC-RNase.d(ACGA) complex was determined at 1.80 A resolution. Residues Lys-9, His-10, Lys-35, and His-103 interacted directly with catalytic phosphate at the P(1) site, and Lys-9 was stabilized by hydrogen bonds contributed by Pyr-1, Tyr-28, and Asn-38. Thr-70 acts as a hydrogen bond donor for cytosine through Thr-39 and determines B(1) base specificity. Interestingly, Pyr-1 along with Lys-95 and Glu-97 form four hydrogen bonds with guanine at B(2) site and determine B(2) base specificity.


==About this Structure==
==About this Structure==
1M07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rana_catesbeiana Rana catesbeiana]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M07 OCA].  
1M07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rana_catesbeiana Rana catesbeiana]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M07 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Amiraslanov, I.]]
[[Category: Amiraslanov, I.]]
[[Category: Chern, S.S.]]
[[Category: Chern, S S.]]
[[Category: Hsiao, Y.Y.]]
[[Category: Hsiao, Y Y.]]
[[Category: Leu, Y.J.]]
[[Category: Leu, Y J.]]
[[Category: Liao, Y.D.]]
[[Category: Liao, Y D.]]
[[Category: Liaw, Y.C.]]
[[Category: Liaw, Y C.]]
[[Category: Wang, S.C.]]
[[Category: Wang, S C.]]
[[Category: bullfrog]]
[[Category: bullfrog]]
[[Category: cytotoxicity]]
[[Category: cytotoxicity]]
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[[Category: ribonuclease]]
[[Category: ribonuclease]]


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