1ILV

Crystal Structure Analysis of the TM107

Summary for 1ILV

• Entry DOI: 10.2210/pdb1ilv/pdb
• Descriptor: STATIONARY-PHASE SURVIVAL PROTEIN SURE HOMOLOG (2 entities in total)
• Functional Keywords: new fold, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function
• Biological source: Thermotoga maritima
• Cellular location: Cytoplasm : P96112
• Total number of polymer chains: 2
• Total formula weight: 57245.77

Authors

Zhang, R.,Joachimiak, A.,Edwards, A.,Savchenko, A.,Beasley, S.,Evdokimova, E.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2001-05-08, release date: 2001-10-10, Last modification date: 2024-11-06)

Primary citation

Zhang, R.G.,Skarina, T.,Katz, J.E.,Beasley, S.,Khachatryan, A.,Vyas, S.,Arrowsmith, C.H.,Clarke, S.,Edwards, A.,Joachimiak, A.,Savchenko, A.
Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase.
Structure, 9:1095-1106, 2001

PubMed Abstract: The rpoS, nlpD, pcm, and surE genes are among many whose expression is induced during the stationary phase of bacterial growth. rpoS codes for the stationary-phase RNA polymerase sigma subunit, and nlpD codes for a lipoprotein. The pcm gene product repairs damaged proteins by converting the atypical isoaspartyl residues back to L-aspartyls. The physiological and biochemical functions of surE are unknown, but its importance in stress is supported by the duplication of the surE gene in E. coli subjected to high-temperature growth. The pcm and surE genes are highly conserved in bacteria, archaea, and plants.

PubMed: 11709173
DOI: 10.1016/S0969-2126(01)00675-X

Experimental method

X-RAY DIFFRACTION (2 Å)