2LFV

Solution Structure of the SPOR domain from E. coli DamX

Summary for 2LFV

• Entry DOI: 10.2210/pdb2lfv/pdb
• NMR Information: BMRB: 17783
• Descriptor: Protein damX (1 entity in total)
• Functional Keywords: cell division, peptidoglycan binding domain, murein binding domain, bacterial cell division protein, rnp fold, rnp domain, cell cycle
• Biological source: Escherichia coli
• Cellular location: Cell membrane; Single-pass membrane protein (Potential): P11557
• Total number of polymer chains: 1
• Total formula weight: 11876.16

Authors

Williams, K.B.,Arends, S.J.R.,Popham, D.L.,Fowler, C.A.,Weiss, D.S. (deposition date: 2011-07-15, release date: 2012-07-18, Last modification date: 2024-05-15)

Primary citation

Williams, K.B.,Yahashiri, A.,Arends, S.J.,Popham, D.L.,Fowler, C.A.,Weiss, D.S.
Nuclear Magnetic Resonance Solution Structure of the Peptidoglycan-Binding SPOR Domain from Escherichia coli DamX: Insights into Septal Localization.
Biochemistry, 52:627-639, 2013

PubMed Abstract: SPOR domains are present in thousands of bacterial proteins and probably bind septal peptidoglycan (PG), but the details of the SPOR-PG interaction have yet to be elucidated. Here we characterize the structure and function of the SPOR domain for an Escherichia coli division protein named DamX. Nuclear magnetic resonance revealed the domain comprises a four-stranded antiparallel β-sheet buttressed on one side by two α-helices. A third helix, designated α3, associates with the other face of the β-sheet, but this helix is relatively mobile. Site-directed mutagenesis revealed the face of the β-sheet that interacts with α3 is important for septal localization and binding to PG sacculi. The position and mobility of α3 suggest it might regulate PG binding, but although α3 deletion mutants still localized to the septal ring, they were too unstable to use in a PG binding assay. Finally, to assess the importance of the SPOR domain in DamX function, we constructed and characterized E. coli mutants that produced DamX proteins with SPOR domain point mutations or SPOR domain deletions. These studies revealed the SPOR domain is important for multiple activities associated with DamX: targeting the protein to the division site, conferring full resistance to the bile salt deoxycholate, improving the efficiency of cell division when DamX is produced at normal levels, and inhibiting cell division when DamX is overproduced.

PubMed: 23290046
DOI: 10.1021/bi301609e

Experimental method

SOLUTION NMR