1J9K

CRYSTAL STRUCTURE OF SURE PROTEIN FROM T.MARITIMA IN COMPLEX WITH TUNGSTATE

Summary for 1J9K

• Entry DOI: 10.2210/pdb1j9k/pdb
• Related: 1J9J 1J9L
• Descriptor: STATIONARY PHASE SURVIVAL PROTEIN, CALCIUM ION, TUNGSTATE(VI)ION, ... (5 entities in total)
• Functional Keywords: tungstate complex, sure protein, unknown function
• Biological source: Thermotoga maritima
• Cellular location: Cytoplasm (Potential): P96112
• Total number of polymer chains: 2
• Total formula weight: 57266.52

Authors

Suh, S.W.,Lee, J.Y.,Kwak, J.E.,Moon, J. (deposition date: 2001-05-27, release date: 2001-09-12, Last modification date: 2023-10-25)

Primary citation

Lee, J.Y.,Kwak, J.E.,Moon, J.,Eom, S.H.,Liong, E.C.,Pedelacq, J.D.,Berendzen, J.,Suh, S.W.
Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family.
Nat.Struct.Biol., 8:789-794, 2001

PubMed Abstract: 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.

PubMed: 11524683
DOI: 10.1038/nsb0901-789

Experimental method

X-RAY DIFFRACTION (2.1 Å)