4A1R
The Structure of Serratia marcescens Lip, a membrane bound component of the Type VI Secretion System.
Summary for 4A1R
| Entry DOI | 10.2210/pdb4a1r/pdb |
| Descriptor | LIP, SODIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | membrane protein, t6ss, beta-sandwich |
| Biological source | SERRATIA MARCESCENS |
| Total number of polymer chains | 4 |
| Total formula weight | 65446.67 |
| Authors | Rao, V.A.,Shepherd, S.M.,English, G.,Coulthurst, S.J.,Hunter, W.N. (deposition date: 2011-09-19, release date: 2011-10-05, Last modification date: 2024-05-01) |
| Primary citation | Rao, V.A.,Shepherd, S.M.,English, G.,Coulthurst, S.J.,Hunter, W.N. The Structure of Serratia Marcescens Lip, a Membrane-Bound Component of the Type Vi Secretion System Acta Crystallogr.,Sect.F, 67:1065-, 2011 Cited by PubMed Abstract: Lip is a membrane-bound lipoprotein and a core component of the type VI secretion system found in Gram-negative bacteria. The structure of a Lip construct (residues 29-176) from Serratia marcescens (SmLip) has been determined at 1.92 Å resolution. Experimental phases were derived using a single-wavelength anomalous dispersion approach on a sample cocrystallized with iodide. The membrane localization of the native protein was confirmed. The structure is that of the globular domain lacking only the lipoprotein signal peptide and the lipidated N-terminus of the mature protein. The protein fold is dominated by an eight-stranded β-sandwich and identifies SmLip as a new member of the transthyretin family of proteins. Transthyretin and the only other member of the family fold, 5-hydroxyisourate hydrolase, form homotetramers important for their function. The asymmetric unit of SmLip is a tetramer with 222 symmetry, but the assembly is distinct from that previously noted for the transthyretin protein family. However, structural comparisons and bacterial two-hybrid data suggest that the SmLip tetramer is not relevant to its role as a core component of the type VI secretion system, but rather reflects a propensity for SmLip to participate in protein-protein interactions. A relatively low level of sequence conservation amongst Lip homologues is noted and is restricted to parts of the structure that might be involved in interactions with physiological partners. PubMed: 22120744DOI: 10.1107/S0907444911046300 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.92 Å) |
Structure validation
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