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2ox3
From Proteopedia
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[[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 [[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]. | |
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| + | ==See Also== | ||
| + | *[[Fructose-1%2C6-bisphosphatase|Fructose-1%2C6-bisphosphatase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <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]] | ||
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| - | ''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
Contents |
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
- 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
- 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:http://dx.doi.org/10.1128/AEM.02220-07
