2v2a: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
2V2A is a | 2V2A 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=2V2A OCA]. | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:18085797</ref><ref group="xtra">PMID:12962479</ref><references group="xtra"/> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Rhamnulose-1-phosphate aldolase]] | [[Category: Rhamnulose-1-phosphate aldolase]] | ||
[[Category: Grueninger, D.]] | [[Category: Grueninger, D.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
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[[Category: Zinc enzyme]] | [[Category: Zinc enzyme]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 11:15:16 2009'' | ||
Revision as of 09:15, 16 February 2009
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A-K248G-R253A-E254A)
Template:ABSTRACT PUBMED 18085797
About this Structure
2V2A is a 1 chain structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Grueninger D, Schulz GE. Antenna domain mobility and enzymatic reaction of L-rhamnulose-1-phosphate aldolase. Biochemistry. 2008 Jan 15;47(2):607-14. Epub 2007 Dec 18. PMID:18085797 doi:https://dx.doi.org/10.1021/bi7012799
- Kroemer M, Merkel I, Schulz GE. Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase. Biochemistry. 2003 Sep 16;42(36):10560-8. PMID:12962479 doi:https://dx.doi.org/10.1021/bi0349266
Page seeded by OCA on Mon Feb 16 11:15:16 2009
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Categories:
- Pages with broken file links
- Escherichia coli
- Rhamnulose-1-phosphate aldolase
- Grueninger, D.
- Schulz, G E.
- 2-ketose degradation
- Aldolase
- Bacterial l-rhamnose metabolism
- Class ii
- Cleavage of l-rhamnulose-1-phosphate to dihydroxyacetone phosphate
- Domain motion for mechanical support of catalysis
- Lyase
- Metal-binding
- Protein engineering
- Protein-protein interface
- Rare sugar
- Rhamnose metabolism
- Surface mutation
- Zinc
- Zinc enzyme