Structural highlights
Function
[SURE_THEMA] Nucleotidase that preferentially dephosphorylates 5'-GMP and 5'-AMP.[HAMAP-Rule:MF_00060]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Homologs of the Escherichia coli surE gene are present in many eubacteria and archaea. Despite the evolutionary conservation, little information is available on the structure and function of their gene products. We have determined the crystal structure of the SurE protein from Thermotoga maritima. The structure reveals the dimeric arrangement of the subunits and an active site around a bound metal ion. We also demonstrate that the SurE protein exhibits a divalent metal ion-dependent phosphatase activity that is inhibited by vanadate or tungstate. In the vanadate- and tungstate-complexed structures, the inhibitors bind adjacent to the divalent metal ion. Our structural and functional analyses identify the SurE proteins as a novel family of metal ion-dependent phosphatases.
Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family.,Lee JY, Kwak JE, Moon J, Eom SH, Liong EC, Pedelacq JD, Berendzen J, Suh SW Nat Struct Biol. 2001 Sep;8(9):789-94. PMID:11524683[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee JY, Kwak JE, Moon J, Eom SH, Liong EC, Pedelacq JD, Berendzen J, Suh SW. Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family. Nat Struct Biol. 2001 Sep;8(9):789-94. PMID:11524683 doi:10.1038/nsb0901-789
