1TM6

NMR Structure of the Free Zinc Binding C-terminal Domain of SecA

Summary for 1TM6

• Entry DOI: 10.2210/pdb1tm6/pdb
• NMR Information: BMRB: 6289
• Descriptor: Preprotein translocase secA subunit, ZINC ION (2 entities in total)
• Functional Keywords: zinc finger, beta hairpin, seca, protein transport
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side: P10408
• Total number of polymer chains: 1
• Total formula weight: 2504.22

Authors

Matousek, W.M.,Alexandrescu, A.T. (deposition date: 2004-06-10, release date: 2004-10-12, Last modification date: 2024-05-22)

Primary citation

Matousek, W.M.,Alexandrescu, A.T.
NMR structure of the C-terminal domain of SecA in the free state
Biochim.Biophys.Acta, 1702:163-171, 2004

PubMed Abstract: SecA is an integral component of the prokaryotic Sec preprotein secretory translocase system. We report here the solution NMR structure of a fragment corresponding to the C-terminal domain of Escherichia coli SecA. In the presence of Zn2+, the fragment adopts a shortened version of the classic betabetaalpha zinc finger fold. The isolated C-terminal domain shows substantial differences from the X-ray structure of a homologous SecA domain bound to the chaperone-like cofactor SecB. The differences between the structures of the free and bound forms suggest that binding to SecB causes a perturbation of the C-terminal domain's intrinsically favored betabetaalpha fold.

PubMed: 15488768
DOI: 10.1016/j.bbapap.2004.08.012

Experimental method

SOLUTION NMR