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1wlj

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==Overview==
==Overview==
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ISG20 is an interferon-induced antiviral exoribonuclease that acts on, single-stranded RNA and also has minor activity towards single-stranded, DNA. It belongs to the DEDDh group of RNases of the DEDD exonuclease, superfamily. We have solved the crystal structure of human ISG20 complexed, with two Mn2+ ions and uridine 5'-monophosphate (UMP) at 1.9 A resolution., Its structure, including that of the active site, is very similar to those, of the corresponding domains of two DEDDh-group DNases, the epsilon, subunit of Escherichia coli DNA polymerase III and E. coli exonuclease I, strongly suggesting that its catalytic mechanism is identical to that of, the two DNases. However, ISG20 also has distinctive residues, Met14 and, Arg53, to accommodate hydrogen bonds with the 2'-OH group of the UMP, ribose, and these residues may be responsible for the preference of ISG20, for RNA substrates.
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ISG20 is an interferon-induced antiviral exoribonuclease that acts on single-stranded RNA and also has minor activity towards single-stranded DNA. It belongs to the DEDDh group of RNases of the DEDD exonuclease superfamily. We have solved the crystal structure of human ISG20 complexed with two Mn2+ ions and uridine 5'-monophosphate (UMP) at 1.9 A resolution. Its structure, including that of the active site, is very similar to those of the corresponding domains of two DEDDh-group DNases, the epsilon subunit of Escherichia coli DNA polymerase III and E. coli exonuclease I, strongly suggesting that its catalytic mechanism is identical to that of the two DNases. However, ISG20 also has distinctive residues, Met14 and Arg53, to accommodate hydrogen bonds with the 2'-OH group of the UMP ribose, and these residues may be responsible for the preference of ISG20 for RNA substrates.
==About this Structure==
==About this Structure==
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[[Category: exoribonuclease]]
[[Category: exoribonuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:07:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:45:40 2008''

Revision as of 13:45, 21 February 2008

Image:1wlj.jpg

1wlj, resolution 1.9Å

Drag the structure with the mouse to rotate

human ISG20

Overview

ISG20 is an interferon-induced antiviral exoribonuclease that acts on single-stranded RNA and also has minor activity towards single-stranded DNA. It belongs to the DEDDh group of RNases of the DEDD exonuclease superfamily. We have solved the crystal structure of human ISG20 complexed with two Mn2+ ions and uridine 5'-monophosphate (UMP) at 1.9 A resolution. Its structure, including that of the active site, is very similar to those of the corresponding domains of two DEDDh-group DNases, the epsilon subunit of Escherichia coli DNA polymerase III and E. coli exonuclease I, strongly suggesting that its catalytic mechanism is identical to that of the two DNases. However, ISG20 also has distinctive residues, Met14 and Arg53, to accommodate hydrogen bonds with the 2'-OH group of the UMP ribose, and these residues may be responsible for the preference of ISG20 for RNA substrates.

About this Structure

1WLJ is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of human ISG20, an interferon-induced antiviral ribonuclease., Horio T, Murai M, Inoue T, Hamasaki T, Tanaka T, Ohgi T, FEBS Lett. 2004 Nov 5;577(1-2):111-6. PMID:15527770

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