2v2b
From Proteopedia
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[[Image:2v2b.png|left|200px]] | [[Image:2v2b.png|left|200px]] | ||
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{{STRUCTURE_2v2b| PDB=2v2b | SCENE= }} | {{STRUCTURE_2v2b| PDB=2v2b | SCENE= }} | ||
===L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E117S-E192A-K248G-R253A-E254A)=== | ===L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E117S-E192A-K248G-R253A-E254A)=== | ||
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{{ABSTRACT_PUBMED_18085797}} | {{ABSTRACT_PUBMED_18085797}} | ||
==About this Structure== | ==About this Structure== | ||
| - | [[2v2b]] 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=2V2B OCA]. | + | [[2v2b]] is a 1 chain structure of [[Aldolase]] 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=2V2B OCA]. |
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| + | ==See Also== | ||
| + | *[[Aldolase|Aldolase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:018085797</ref><ref group="xtra">PMID:018187656</ref><ref group="xtra">PMID:012962479</ref><references group="xtra"/> |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Rhamnulose-1-phosphate aldolase]] | [[Category: Rhamnulose-1-phosphate aldolase]] | ||
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[[Category: Rhamnose metabolism]] | [[Category: Rhamnose metabolism]] | ||
[[Category: Surface mutation]] | [[Category: Surface mutation]] | ||
| - | [[Category: Zinc]] | ||
[[Category: Zinc enzyme]] | [[Category: Zinc enzyme]] | ||
Revision as of 20:10, 25 July 2012
Contents |
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E117S-E192A-K248G-R253A-E254A)
Template:ABSTRACT PUBMED 18085797
About this Structure
2v2b is a 1 chain structure of Aldolase with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
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:http://dx.doi.org/10.1021/bi7012799
- Grueninger D, Treiber N, Ziegler MO, Koetter JW, Schulze MS, Schulz GE. Designed protein-protein association. Science. 2008 Jan 11;319(5860):206-9. PMID:18187656 doi:http://dx.doi.org/319/5860/206
- 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:http://dx.doi.org/10.1021/bi0349266
Categories: 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 enzyme
