3v3w

Crystal structure of an enolase from the soil bacterium Cellvibrio japonicus (TARGET EFI-502161) with bound MG and glycerolCrystal structure of an enolase from the soil bacterium Cellvibrio japonicus (TARGET EFI-502161) with bound MG and glycerol

Structural highlights

3v3w is a 1 chain structure with sequence from Cellvibrio japonicus Ueda107. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.4Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MAND_CELJU Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).^[1]

References

↑ Wichelecki DJ, Balthazor BM, Chau AC, Vetting MW, Fedorov AA, Fedorov EV, Lukk T, Patskovsky YV, Stead MB, Hillerich BS, Seidel RD, Almo SC, Gerlt JA. Discovery of function in the enolase superfamily: D-mannonate and d-gluconate dehydratases in the D-mannonate dehydratase subgroup. Biochemistry. 2014 Apr 29;53(16):2722-31. doi: 10.1021/bi500264p. Epub 2014 Apr, 15. PMID:24697546 doi:http://dx.doi.org/10.1021/bi500264p

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OCA

[1] Wichelecki DJ, Balthazor BM, Chau AC, Vetting MW, Fedorov AA, Fedorov EV, Lukk T, Patskovsky YV, Stead MB, Hillerich BS, Seidel RD, Almo SC, Gerlt JA. Discovery of function in the enolase superfamily: D-mannonate and d-gluconate dehydratases in the D-mannonate dehydratase subgroup. Biochemistry. 2014 Apr 29;53(16):2722-31. doi: 10.1021/bi500264p. Epub 2014 Apr, 15. PMID:24697546 doi:http://dx.doi.org/10.1021/bi500264p

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