2v29
From Proteopedia
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT K15W)
Template:ABSTRACT PUBMED 18085797
About this Structure
2V29 is a 2 chains structure of sequences 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:http://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:http://dx.doi.org/10.1021/bi0349266
Page seeded by OCA on Mon Feb 16 16:26:01 2009
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 | Zinc enzyme
