4GJI: Crystal Structure Of Pseudomonas Stutzeri L-rhamnose Isomerase Mutant H101n In Complex With L-rhamnopyranose

Citation:
Abstract
l-Rhamnose isomerase (l-RhI) catalyzes the reversible isomerization of l-rhamnose to l-rhamnulose. Previously determined X-ray structures of l-RhI showed a hydride-shift mechanism for the isomerization of substrates in a linear form, but the mechanism for opening of the sugar-ring is still unclear. To elucidate this mechanism, we determined X-ray structures of a mutant l-RhI in complex with l-rhamnopyranose and d-allopyranose. Results suggest that a catalytic water molecule, which acts as an acid/base catalyst in the isomerization reaction, is likely to be involved in pyranose-ring opening, and that a newly found substrate sub-binding site in the vicinity of the catalytic site may recognize different anomers of substrates.
PDB ID: 4GJIDownload
MMDB ID: 105793
PDB Deposition Date: 2012/8/9
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 1.7  Å
Source Organism:
Similar Structures:
Biological Unit for 4GJI: tetrameric; determined by author and by software (PISA)
Molecular Components in 4GJI
Label Count Molecule
Proteins (4 molecules)
4
L-rhamnose Isomerase
Molecule annotation
Chemicals (21 molecules)
1
4
2
4
3
10
4
3
* Click molecule labels to explore molecular sequence information.

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