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4nyn

From Proteopedia

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m (Protected "4nyn" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4nyn| PDB=4nyn | SCENE= }}
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===Crystal structure of RNase H1 from halophilic archaeon Halobacterium salinarum NRC-1===
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The entry 4nyn is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/RNH_HALSA RNH_HALSA]] Nuclease that specifically degrades the RNA of RNA-DNA hybrids; seems to act exonucleolytically on RNA/DNA hybrids. Endonucleolytically removes RNA primers from the Okazaki fragments of lagging strand synthesis on its own. Complements the temperature-sensitive phenotype of an E.coli double rnhA/rnhB (RNase H) disruption mutant.<ref>PMID:15115438</ref>
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Authors: You, D.J., Angkawidjaja, C., Koga, Y., Kanaya, S.
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==About this Structure==
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[[4nyn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NYN OCA].
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Description: Crystal structure of RNase H1 from halophilic archaeon Halobacterium salinarum NRC-1
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Ribonuclease H]]
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[[Category: Angkawidjaja, C.]]
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[[Category: Kanaya, S.]]
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[[Category: Koga, Y.]]
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[[Category: You, D J.]]
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[[Category: Hydrolase]]
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[[Category: Rnase h1]]

Revision as of 05:24, 13 February 2014

Template:STRUCTURE 4nyn

Contents

Crystal structure of RNase H1 from halophilic archaeon Halobacterium salinarum NRC-1

Function

[RNH_HALSA] Nuclease that specifically degrades the RNA of RNA-DNA hybrids; seems to act exonucleolytically on RNA/DNA hybrids. Endonucleolytically removes RNA primers from the Okazaki fragments of lagging strand synthesis on its own. Complements the temperature-sensitive phenotype of an E.coli double rnhA/rnhB (RNase H) disruption mutant.[1]

About this Structure

4nyn is a 2 chain structure. Full crystallographic information is available from OCA.

Reference

  1. ↑ Ohtani N, Yanagawa H, Tomita M, Itaya M. Identification of the first archaeal Type 1 RNase H gene from Halobacterium sp. NRC-1: archaeal RNase HI can cleave an RNA-DNA junction. Biochem J. 2004 Aug 1;381(Pt 3):795-802. PMID:15115438 doi:http://dx.doi.org/10.1042/BJ20040153

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