4nci

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m (Protected "4nci" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4nci| PDB=4nci | SCENE= }}
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===Crystal Structure of Pyrococcus furiosis Rad50 R805E mutation===
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{{ABSTRACT_PUBMED_24493214}}
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The entry 4nci is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/RAD50_PYRFU RAD50_PYRFU]] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449]
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Authors: Classen, S., Williams, G.J., Arvai, A.S., Williams, R.S.
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==About this Structure==
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[[4nci]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NCI OCA].
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Description: Crystal Structure of Pyrococcus furiosis Rad50 R805E mutation
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==Reference==
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<ref group="xtra">PMID:024493214</ref><references group="xtra"/><references/>
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[[Category: Arvai, A S.]]
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[[Category: Classen, S.]]
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[[Category: Williams, G J.]]
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[[Category: Williams, R S.]]
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[[Category: Adenosine triphosphatase]]
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[[Category: Dna binding protein]]
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[[Category: Dna repair]]
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[[Category: Fungal protein]]

Revision as of 07:27, 2 April 2014

Template:STRUCTURE 4nci

Contents

Crystal Structure of Pyrococcus furiosis Rad50 R805E mutation

Template:ABSTRACT PUBMED 24493214

Function

[RAD50_PYRFU] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449]

About this Structure

4nci is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  • Deshpande RA, Williams GJ, Limbo O, Williams RS, Kuhnlein J, Lee JH, Classen S, Guenther G, Russell P, Tainer JA, Paull TT. ATP-driven Rad50 conformations regulate DNA tethering, end resection, and ATM checkpoint signaling. EMBO J. 2014 Mar 3;33(5):482-500. doi: 10.1002/embj.201386100. Epub 2014 Feb 3. PMID:24493214 doi:http://dx.doi.org/10.1002/embj.201386100

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OCA

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