2ox3: Difference between revisions

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{{Seed}}
[[Image:2ox3.png|left|200px]]
[[Image:2ox3.png|left|200px]]


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{{STRUCTURE_2ox3|  PDB=2ox3  |  SCENE=  }}  
{{STRUCTURE_2ox3|  PDB=2ox3  |  SCENE=  }}  


===R-state, PEP and Fru-6-P-bound, Escherichia coli fructose-1,6-bisphosphatase===
===R-state, PEP and Fru-6-P-bound, Escherichia coli fructose-1,6-bisphosphatase===


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{{ABSTRACT_PUBMED_17314096}}
{{ABSTRACT_PUBMED_17314096}}


==About this Structure==
==About this Structure==
2OX3 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=2OX3 OCA].  
[[2ox3]] is a 1 chain structure of [[Fructose-1%2C6-bisphosphatase]] 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=2OX3 OCA].  
 
==See Also==
*[[Fructose-1%2C6-bisphosphatase|Fructose-1%2C6-bisphosphatase]]


==Reference==
==Reference==
<ref group="xtra">PMID:17314096</ref><references group="xtra"/>
<ref group="xtra">PMID:017314096</ref><ref group="xtra">PMID:018156340</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Fructose-bisphosphatase]]
[[Category: Fructose-bisphosphatase]]
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[[Category: Glycolysis]]
[[Category: Glycolysis]]
[[Category: Gram-negative]]
[[Category: Gram-negative]]
[[Category: Hydrolase]]
[[Category: Protein crystallography]]
[[Category: Protein crystallography]]
[[Category: Protein-protein interaction]]
[[Category: Protein-protein interaction]]
[[Category: Proteobacteria]]
[[Category: Proteobacteria]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 09:21:22 2009''

Revision as of 15:35, 27 July 2012

File:2ox3.png

Template:STRUCTURE 2ox3

R-state, PEP and Fru-6-P-bound, Escherichia coli fructose-1,6-bisphosphatase

Template:ABSTRACT PUBMED 17314096

About this Structure

2ox3 is a 1 chain structure of Fructose-1,6-bisphosphatase with sequence from Escherichia coli. Full crystallographic information is available from OCA.

See Also

Reference

  1. Hines JK, Fromm HJ, Honzatko RB. Structures of activated fructose-1,6-bisphosphatase from Escherichia coli. Coordinate regulation of bacterial metabolism and the conservation of the R-state. J Biol Chem. 2007 Apr 20;282(16):11696-704. Epub 2007 Feb 21. PMID:17314096 doi:10.1074/jbc.M611104200
  2. Xiao Z, Bergeron H, Grosse S, Beauchemin M, Garron ML, Shaya D, Sulea T, Cygler M, Lau PC. Improvement of the thermostability and activity of a pectate lyase by single amino acid substitutions, using a strategy based on melting-temperature-guided sequence alignment. Appl Environ Microbiol. 2008 Feb;74(4):1183-9. Epub 2007 Dec 21. PMID:18156340 doi:https://dx.doi.org/10.1128/AEM.02220-07

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