4GJI

Crystal structure of Pseudomonas stutzeri L-rhamnose isomerase mutant H101N in complex with L-rhamnopyranose

Summary for 4GJI

• Entry DOI: 10.2210/pdb4gji/pdb
• Related: 2HCV 2I56 4GJJ
• Descriptor: L-rhamnose isomerase, L-RHAMNOSE, alpha-L-rhamnopyranose, ... (6 entities in total)
• Functional Keywords: tim barrel, isomerase, sugar binding, metal binding
• Biological source: Pseudomonas stutzeri
• Total number of polymer chains: 4
• Total formula weight: 194277.38

Authors

Yoshida, H.,Kamitori, S. (deposition date: 2012-08-09, release date: 2012-12-12, Last modification date: 2023-11-08)

Primary citation

Yoshida, H.,Yoshihara, A.,Teraoka, M.,Yamashita, S.,Izumori, K.,Kamitori, S.
Structure of l-rhamnose isomerase in complex with l-rhamnopyranose demonstrates the sugar-ring opening mechanism and the role of a substrate sub-binding site.
FEBS Open Bio, 3:35-40, 2013

PubMed 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.

PubMed: 23772372
DOI: 10.1016/j.fob.2012.11.008

Experimental method

X-RAY DIFFRACTION (1.7 Å)