2WQ0

GCN4 leucine zipper mutant with three IxxNTxx motifs coordinating chloride

Summary for 2WQ0

• Entry DOI: 10.2210/pdb2wq0/pdb
• Related: 1CE9 1DGC 1GCL 1GCM 1GZL 1IHQ 1IJ0 1IJ1 1IJ2 1IJ3 1KQL 1LD4 1LLM 1NKN 1PIQ 1RB1 1RB4 1RB5 1RB6 1SWI 1TMZ 1UNT 1UNU 1UNV 1UNW 1UNX 1UNY 1UNZ 1UO0 1UO1 1UO2 1UO3 1UO4 1UO5 1W5G 1W5H 1W5I 1W5J 1W5K 1W5L 1YSA 1ZII 1ZIJ 1ZIK 1ZIL 1ZIM 1ZTA 2B1F 2B22 2BNI 2CCE 2CCF 2CCN 2D3E 2DGC 2WG5 2WG6 2WPQ 2WPR 2WPS 2WPY 2WPZ 2WQ1 2WQ2 2WQ3 2ZTA
• Descriptor: GENERAL CONTROL PROTEIN GCN4, CHLORIDE ION (3 entities in total)
• Functional Keywords: taa, nucleus, coiled coil, dna-binding, protein export, ion coordination, polar core residues, trimeric autotransporter adhesin, transcription
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Nucleus: P03069
• Total number of polymer chains: 1
• Total formula weight: 4073.83

Authors

Hartmann, M.D.,Hernandez Alvarez, B.,Lupas, A.N. (deposition date: 2009-08-12, release date: 2009-11-03, Last modification date: 2023-12-20)

Primary citation

Hartmann, M.D.,Ridderbusch, O.,Zeth, K.,Albrecht, R.,Testa, O.,Woolfson, D.N.,Sauer, G.,Dunin-Horkawicz, S.,Lupas, A.N.,Alvarez, B.H.
A Coiled-Coil Motif that Sequesters Ions to the Hydrophobic Core.
Proc.Natl.Acad.Sci.USA, 106:16950-, 2009

PubMed Abstract: Most core residues of coiled coils are hydrophobic. Occasional polar residues are thought to lower stability, but impart structural specificity. The coiled coils of trimeric autotransporter adhesins (TAAs) are conspicuous for their large number of polar residues in position d of the core, which often leads to their prediction as natively unstructured regions. The most frequent residue, asparagine (N@d), can occur in runs of up to 19 consecutive heptads, frequently in the motif [I/V]xxNTxx. In the Salmonella TAA, SadA, the core asparagines form rings of interacting residues with the following threonines, grouped around a central anion. This conformation is observed generally in N@d layers from trimeric coiled coils of known structure. Attempts to impose a different register on the motif show that the asparagines orient themselves specifically into the core, even against conflicting information from flanking domains. When engineered into the GCN4 leucine zipper, N@d layers progressively destabilized the structure, but zippers with 3 N@d layers still folded at high concentration. We propose that N@d layers maintain the coiled coils of TAAs in a soluble, export-competent state during autotransport through the outer membrane. More generally, we think that polar motifs that are both periodic and conserved may often reflect special folding requirements, rather than an unstructured state of the mature proteins.

PubMed: 19805097
DOI: 10.1073/PNAS.0907256106

Experimental method

X-RAY DIFFRACTION (1.12 Å)