1oie

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{{Seed}}
 
[[Image:1oie.png|left|200px]]
[[Image:1oie.png|left|200px]]
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==About this Structure==
==About this Structure==
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1OIE is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OIE OCA].
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[[1oie]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OIE OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:15215524</ref><references group="xtra"/>
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<ref group="xtra">PMID:15215524</ref><ref group="xtra">PMID:11491294</ref><ref group="xtra">PMID:10331872</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Maier, T.]]
[[Category: Maier, T.]]
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[[Category: Metalloprotein]]
[[Category: Metalloprotein]]
[[Category: Periplasmic]]
[[Category: Periplasmic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 22:34:16 2009''
 

Revision as of 00:28, 15 March 2011

Template:STRUCTURE 1oie

5'-NUCLEOTIDASE (E. COLI) WITH AN ENGINEERED DISULFIDE BRIDGE (S228C, P513C)

Template:ABSTRACT PUBMED 15215524

About this Structure

1oie is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Schultz-Heienbrok R, Maier T, Strater N. Trapping a 96 degrees domain rotation in two distinct conformations by engineered disulfide bridges. Protein Sci. 2004 Jul;13(7):1811-22. PMID:15215524 doi:10.1110/ps.04629604
  • Knofel T, Strater N. E. coli 5'-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion. J Mol Biol. 2001 May 25;309(1):255-66. PMID:11491294 doi:S0022-2836(01)94657-1
  • Knofel T, Strater N. X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site. Nat Struct Biol. 1999 May;6(5):448-53. PMID:10331872 doi:10.1038/8253

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