4FUM

Structural basis for Zn2+-dependent intercellular adhesion in staphylococcal biofilms

Summary for 4FUM

• Entry DOI: 10.2210/pdb4fum/pdb
• Related: 4FUN 4FUO 4FUP
• Descriptor: Accumulation associated protein, ZINC ION, THIOCYANATE ION, ... (4 entities in total)
• Functional Keywords: hydrophilic protein, non-globular, freestanding beta sheet, intercellular adhesion, zinc dependent dimer, membrane protein
• Biological source: Staphylococcus epidermidis
• Cellular location: Secreted, cell wall; Peptidoglycan-anchor (By similarity): Q5HKE8
• Total number of polymer chains: 1
• Total formula weight: 22695.80

Authors

Conrady, D.G.,Wilson, J.J.,Herr, A.B. (deposition date: 2012-06-28, release date: 2013-01-16, Last modification date: 2024-11-06)

Primary citation

Conrady, D.G.,Wilson, J.J.,Herr, A.B.
Structural basis for Zn2+-dependent intercellular adhesion in staphylococcal biofilms.
Proc.Natl.Acad.Sci.USA, 110:E202-E211, 2013

PubMed Abstract: Staphylococcal bacteria, including Staphylococcus epidermidis and Staphylococcus aureus, cause chronic biofilm-related infections. The homologous proteins Aap and SasG mediate biofilm formation in S. epidermidis and S. aureus, respectively. The self-association of these proteins in the presence of Zn(2+) leads to the formation of extensive adhesive contacts between cells. This study reports the crystal structure of a Zn(2+) -bound construct from the self-associating region of Aap. Several unusual structural features include elongated β-sheets that are solvent-exposed on both faces and the lack of a canonical hydrophobic core. Zn(2+)-dependent dimers are observed in three distinct crystal forms, formed via pleomorphic coordination of Zn(2+) in trans across the dimer interface. These structures illustrate how a long, flexible surface protein is able to form tight intercellular adhesion sites under adverse environmental conditions.

PubMed: 23277549
DOI: 10.1073/pnas.1208134110

Experimental method

X-RAY DIFFRACTION (2.4 Å)