5BND

Crystal structure of the C-terminal domain of TagH

Summary for 5BND

• Entry DOI: 10.2210/pdb5bnd/pdb
• Descriptor: ABC transporter, ATP-binding protein (2 entities in total)
• Functional Keywords: transporter, transport protein
• Biological source: Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
• Total number of polymer chains: 3
• Total formula weight: 62949.00

Authors

Chen, S.C.,Chen, Y. (deposition date: 2015-05-26, release date: 2016-07-06, Last modification date: 2024-03-20)

Primary citation

Ko, T.P.,Tseng, S.T.,Lai, S.J.,Chen, S.C.,Guan, H.H.,Yang, C.S.,Chen, C.J.,Chen, Y.
SH3-Like Motif-Containing C-terminal Domain of Staphylococcal Teichoic Acid Transporter Suggests Possible Function.
Proteins, 2016

PubMed Abstract: The negatively charged bacterial polysaccharides-wall teichoic acids (WTAs) are synthesized intracellularly and exported by a two-component transporter, TagGH, comprising a transmembrane subunit TagG and an ATPase subunit TagH. We determined the crystal structure of the C-terminal domain of TagH (TagH-C) to investigate its function. The structure shows an N-terminal SH3-like subdomain wrapped by a C-terminal subdomain with an anti-parallel β-sheet and an outer shell of α-helices. A stretch of positively charged surface across the subdomain interface is flanked by two negatively charged regions, suggesting a potential binding site for negatively charged polymers, such as WTAs or acidic peptide chains. Proteins 2016; 84:1328-1332. © 2016 Wiley Periodicals, Inc.

PubMed: 27213893
DOI: 10.1002/prot.25074

Experimental method

X-RAY DIFFRACTION (2.68 Å)